Arenavirus Stable Signal Peptide Is the Keystone Subunit for Glycoprotein Complex Organization

The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity....

Full description

Saved in:

Bibliographic Details
Published in:	mBio Vol. 5; no. 6; p. e02063
Main Authors:	Bederka, Lydia H., Bonhomme, Cyrille J., Ling, Emily L., Buchmeier, Michael J.
Format:	Journal Article
Language:	English
Published:	United States American Society for Microbiology 31.12.2014 American Society of Microbiology
Subjects:	Amino acids Animals Antibodies biosynthesis Cell Line Cell Membrane - chemistry Cell Membrane - virology Cell membranes Confocal microscopy Endoplasmic reticulum Endosomes Enzymes fever Flow Cytometry Genomes Glycoproteins Glycoproteins - metabolism Golgi apparatus Hemorrhagic fever Humans Immunoprecipitation Infectivity Internalization Lymphocytic choriomeningitis mammarenavirus Lymphocytic choriomeningitis virus - physiology Maturation Membrane fusion Membrane trafficking Microscopy Microscopy, Confocal Molecular Biology Mutation pathogenicity pathogens Peptides pH effects plasma membrane polypeptides precipitin tests Protein Multimerization Protein Processing, Post-Translational Protein Sorting Signals Protein Subunits - metabolism Protein Transport Proteins Proteolysis receptors RNA polymerase rodents signal peptide Viral Structural Proteins - metabolism virion Virions Viruses
ISSN:	2161-2129, 2150-7511, 2150-7511
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Abstract	The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex. IMPORTANCE Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation. Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation.
AbstractList	The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex.IMPORTANCE Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation. The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex. Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation. The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex. IMPORTANCE Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation. Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation. The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex. Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation. The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex.UNLABELLEDThe rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex.Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation.IMPORTANCESeveral members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation. ABSTRACT The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex. IMPORTANCE Several members of the Arenaviridae family are neglected human pathogens capable of causing illness ranging from a nondescript flu-like syndrome to fulminant hemorrhagic fever. Infections by arenaviruses are mediated by attachment of the virus glycoprotein to receptors on host cells and virion internalization by fusion within an acidified endosome. SSP plays a critical role in the fusion of the virus with the host cell membrane. Within infected cells, the retained glycoprotein SSP plays a neglected yet essential role in glycoprotein biosynthesis. Without this 6-kDa polypeptide, the glycoprotein precursor is retained within the endoplasmic reticulum, and trafficking to the plasma membrane where SSP, GP1, and GP2 localize for glycoprotein assembly into infectious virions is inhibited. To investigate SSP contributions to glycoprotein maturation and function, we created an SSP-tagged glycoprotein to directly detect and manipulate this subunit. This resource will aid future studies to identify host factors that mediate glycoprotein maturation. The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex.
Author	Bonhomme, Cyrille J. Ling, Emily L. Buchmeier, Michael J. Bederka, Lydia H.
Author_xml	– sequence: 1 givenname: Lydia H. surname: Bederka fullname: Bederka, Lydia H. organization: Department of Molecular Biology & Biochemistry, University of California Irvine, Irvine, California, USA – sequence: 2 givenname: Cyrille J. surname: Bonhomme fullname: Bonhomme, Cyrille J. organization: Department of Molecular Biology & Biochemistry, University of California Irvine, Irvine, California, USA – sequence: 3 givenname: Emily L. surname: Ling fullname: Ling, Emily L. organization: Department of Molecular Biology & Biochemistry, University of California Irvine, Irvine, California, USA – sequence: 4 givenname: Michael J. surname: Buchmeier fullname: Buchmeier, Michael J. organization: Department of Molecular Biology & Biochemistry, University of California Irvine, Irvine, California, USA, Division of Infectious Disease, Department of Medicine, University of California Irvine, Irvine, California, USA
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/25352624$$D View this record in MEDLINE/PubMed
BookMark	eNqFks1rFDEYxgep2Fp79CoDXrxMzfdkLkJdtC4WKqxeDUnmzTbLbLImmeL61zu724otgrkkJM_7y5s8z_PqKMQAVfUSo3OMiXy7fu_jOSJI0AazJ9UJwRw1Lcf4aLcWuCGYdMfVWc4rNA1KsaToWXVMOOVEEHZSfb9IEPStT2OuF0WbAeqFXwY91F9gU3wP9TzX5Qbqz7DNZbq9XoxmDL7ULqb6ctjauEmxgA_1LK43A_ysr9NSB_9LFx_Di-qp00OGs7v5tPr28cPX2afm6vpyPru4aiyXqDSSSwet66XDwpqWI-OkM4xaYEY4qqWFXjhuOuixbREG2lmrBaJ91yNiBD2t5gduH_VKbZJf67RVUXu134hpqXQq3g6gNOVW9kbSVgLrmJBMGt1ZKoUmneu7ifXuwNqMZg29hVCSHh5AH54Ef6OW8VYxglss0QR4cwdI8ccIuai1zxaGQQeIY1a4ZYKhFhP8f6nAUhIuMZ-krx9JV3FMk1NZUSIoazuJdh_x6u_m_3R97_gkoAeBTTHnBE5ZX_ZeTW_xg8JI7aKldtFS-2gpvKtqHlXdg_-t_w2fq9Dq
CitedBy_id	crossref_primary_10_1038_s41598_020_63640_1 crossref_primary_10_1128_JVI_01741_19 crossref_primary_10_1073_pnas_1603364113 crossref_primary_10_1007_s12250_016_3815_4 crossref_primary_10_1080_17460441_2024_2340494 crossref_primary_10_3390_pathogens8010001 crossref_primary_10_1002_chem_202403608 crossref_primary_10_1016_j_apsb_2020_02_014 crossref_primary_10_1128_JVI_02221_20 crossref_primary_10_3389_fimmu_2019_02499 crossref_primary_10_1128_JVI_00574_17 crossref_primary_10_1080_10409238_2025_2503746 crossref_primary_10_1371_journal_ppat_1005418 crossref_primary_10_2217_fvl_15_41 crossref_primary_10_1016_j_ejcb_2018_06_003 crossref_primary_10_1016_j_meegid_2024_105626 crossref_primary_10_1128_JVI_01154_16 crossref_primary_10_1038_s41586_022_04429_2 crossref_primary_10_1128_JVI_00954_18 crossref_primary_10_3390_v14122649 crossref_primary_10_1371_journal_ppat_1009488 crossref_primary_10_3390_math11214454 crossref_primary_10_1016_j_antiviral_2019_03_014 crossref_primary_10_1128_spectrum_03651_23 crossref_primary_10_3390_v17060809 crossref_primary_10_1038_s41467_024_51606_0 crossref_primary_10_1016_j_chom_2025_07_020 crossref_primary_10_1007_s00284_025_04320_z crossref_primary_10_1007_s00784_023_05399_z crossref_primary_10_3390_v17010117 crossref_primary_10_3390_v13071229 crossref_primary_10_3390_molecules28041579 crossref_primary_10_1042_BSR20211930 crossref_primary_10_1128_JVI_01277_19 crossref_primary_10_3390_v12040386 crossref_primary_10_1016_j_bbamem_2022_184031 crossref_primary_10_1128_spectrum_01913_22 crossref_primary_10_1038_s41564_025_02085_6
Cites_doi	10.1128/JVI.07241-11 10.1038/nature05539 10.1128/JVI.00499-07 10.1099/vir.0.80473-0 10.1006/viro.2000.0357 10.1016/j.chom.2013.10.010 10.1128/JVI.01837-10 10.1038/nprot.2007.132 10.1128/JVI.00208-06 10.1074/jbc.M009613200 10.1128/JVI.77.19.10700-10705.2003 10.1038/sj.embor.7400002 10.1056/NEJMoa053240 10.1128/JVI.80.8.4191-4195.2006 10.1128/mBio.00180-12 10.1074/jbc.M312975200 10.1128/JVI.02779-06 10.1074/jbc.M302343200 10.1016/0042-6822(89)90610-7 10.1128/JVI.01481-07 10.1128/JVI.02759-06 10.1016/S0002-9394(00)00570-5 10.1016/j.virol.2010.10.011 10.1099/vir.0.82950-0 10.1089/vbz.2011.0892 10.1073/pnas.1113643108 10.1074/jbc.M101638200 10.1128/JVI.02545-05 10.1016/0042-6822(88)90616-2 10.1186/1743-422X-5-161 10.1016/S0042-6822(03)00421-5 10.1016/j.virol.2012.10.038 10.1128/JVI.02410-08 10.1016/0042-6822(83)90135-6 10.1128/JVI.75.2.1061-1064.2001 10.1016/j.mib.2008.06.001 10.1016/j.virol.2006.08.048 10.1016/0378-1119(91)90434-D 10.1073/pnas.221447598 10.1128/JVI.02146-06 10.1016/0042-6822(81)90137-9 10.1128/JVI.77.5.2866-2872.2003 10.1126/science.1252480 10.1006/viro.1994.1057 10.1128/JVI.78.19.10783-10792.2004 10.1016/S0962-8924(98)01360-9 10.1128/jvi.52.3.897-904.1984 10.1016/j.febslet.2010.09.032 10.1126/scitranslmed.3006827 10.1006/viro.1995.1225 10.1126/science.282.5396.2079
ContentType	Journal Article
Copyright	Copyright © 2014 Bederka et al. 2014. This work is published under http://creativecommons.org/licenses/by-nc-sa/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. Copyright © 2014 Bederka et al. 2014 Bederka et al.
Copyright_xml	– notice: Copyright © 2014 Bederka et al. – notice: 2014. This work is published under http://creativecommons.org/licenses/by-nc-sa/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: Copyright © 2014 Bederka et al. 2014 Bederka et al.
DBID	AAYXX CITATION CGR CUY CVF ECM EIF NPM 8C1 8FE 8FH ABUWG AFKRA AZQEC BBNVY BENPR BHPHI CCPQU COVID DWQXO FYUFA GHDGH GNUQQ HCIFZ LK8 M7P PHGZM PHGZT PIMPY PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS 7X8 7S9 L.6 5PM DOA
DOI	10.1128/mBio.02063-14
DatabaseName	CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Public Health Database ProQuest SciTech Collection ProQuest Natural Science Collection ProQuest Central (Alumni Edition) ProQuest Central UK/Ireland ProQuest Central Essentials Biological Science Collection ProQuest Central Natural Science Collection ProQuest One Community College Coronavirus Research Database ProQuest Central Korea Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student SciTech Premium Collection ProQuest Biological Science Collection Biological Science Database ProQuest Central Premium ProQuest One Academic (New) Publicly Available Content Database ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic AGRICOLA AGRICOLA - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Publicly Available Content Database ProQuest Central Student ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Central China ProQuest Central ProQuest One Applied & Life Sciences ProQuest Health & Medical Research Collection Health Research Premium Collection Natural Science Collection ProQuest Central Korea Health & Medical Research Collection Biological Science Collection ProQuest Central (New) ProQuest Public Health ProQuest Biological Science Collection ProQuest One Academic Eastern Edition Coronavirus Research Database Health Research Premium Collection (Alumni) Biological Science Database ProQuest SciTech Collection ProQuest One Academic UKI Edition ProQuest One Academic ProQuest One Academic (New) MEDLINE - Academic AGRICOLA AGRICOLA - Academic
DatabaseTitleList	Publicly Available Content Database CrossRef MEDLINE MEDLINE - Academic AGRICOLA
Database_xml	– sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: PIMPY name: Publicly Available Content Database url: http://search.proquest.com/publiccontent sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Biology
DocumentTitleAlternate	Arenavirus SSP and Glycoprotein Maturation
EISSN	2150-7511
ExternalDocumentID	oai_doaj_org_article_a35c8db8378e4946848ba9c386a29fd9 PMC4217180 25352624 10_1128_mBio_02063_14
Genre	Research Support, U.S. Gov't, Non-P.H.S Journal Article Research Support, N.I.H., Extramural
GrantInformation_xml	– fundername: NIAID NIH HHS grantid: AI-065359 – fundername: NIAID NIH HHS grantid: U54 AI065359
GroupedDBID	--- 0R~ 53G 5VS 8C1 AAFWJ AAGFI AAUOK AAYXX ABUWG ADBBV ADRAZ AENEX AFFHD AFKRA AFPKN ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BBNVY BCNDV BENPR BHPHI BTFSW CCPQU CITATION DIK E3Z EBS EJD FRP FYUFA GROUPED_DOAJ GX1 H13 HCIFZ HYE HZ~ KQ8 M48 M7P O5R O5S O9- OK1 P2P PGMZT PHGZM PHGZT PIMPY PJZUB PPXIY PQGLB RHI RNS RPM RSF UKHRP CGR CUY CVF ECM EIF M~E NPM RHF 8FE 8FH AZQEC COVID DWQXO GNUQQ LK8 PKEHL PQEST PQQKQ PQUKI PRINS 7X8 7S9 L.6 5PM
ID	FETCH-LOGICAL-c580t-858fe7fd8f16cb750bf8fb43ce4b6f3a8ced6f5b9ed1c701e39cca603d9d02b63
IEDL.DBID	M7P
ISICitedReferencesCount	46
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000347073600035&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	2161-2129 2150-7511
IngestDate	Fri Oct 03 12:53:45 EDT 2025 Tue Nov 04 01:55:47 EST 2025 Fri Jul 11 07:34:00 EDT 2025 Sun Nov 09 13:48:13 EST 2025 Sat Oct 25 01:45:18 EDT 2025 Wed Feb 19 02:31:34 EST 2025 Sat Nov 29 03:10:44 EST 2025 Tue Nov 18 20:45:57 EST 2025
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	6
Language	English
License	Copyright © 2014 Bederka et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited.
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c580t-858fe7fd8f16cb750bf8fb43ce4b6f3a8ced6f5b9ed1c701e39cca603d9d02b63
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Present address: Cyrille J. Bonhomme, PPD, Vaccine Sciences Department, Richmond, Virginia, USA; Emily L. Ling, Department of Art as Applied to Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. This article is a direct contribution from a Fellow of the American Academy of Microbiology. Editor Terence S. Dermody, Vanderbilt University School of Medicine
OpenAccessLink	https://www.proquest.com/docview/3263479806?pq-origsite=%requestingapplication%
PMID	25352624
PQID	3263479806
PQPubID	7421146
ParticipantIDs	doaj_primary_oai_doaj_org_article_a35c8db8378e4946848ba9c386a29fd9 pubmedcentral_primary_oai_pubmedcentral_nih_gov_4217180 proquest_miscellaneous_1746407121 proquest_miscellaneous_1618825815 proquest_journals_3263479806 pubmed_primary_25352624 crossref_citationtrail_10_1128_mBio_02063_14 crossref_primary_10_1128_mBio_02063_14
PublicationCentury	2000
PublicationDate	20141231
PublicationDateYYYYMMDD	2014-12-31
PublicationDate_xml	– month: 12 year: 2014 text: 20141231 day: 31
PublicationDecade	2010
PublicationPlace	United States
PublicationPlace_xml	– name: United States – name: Washington – name: 1752 N St., N.W., Washington, DC
PublicationTitle	mBio
PublicationTitleAlternate	mBio
PublicationYear	2014
Publisher	American Society for Microbiology American Society of Microbiology
Publisher_xml	– name: American Society for Microbiology – name: American Society of Microbiology
References	e_1_3_3_50_2 e_1_3_3_16_2 e_1_3_3_18_2 e_1_3_3_39_2 e_1_3_3_12_2 e_1_3_3_37_2 e_1_3_3_14_2 e_1_3_3_35_2 e_1_3_3_56_2 e_1_3_3_33_2 e_1_3_3_54_2 e_1_3_3_10_2 e_1_3_3_31_2 e_1_3_3_52_2 e_1_3_3_40_2 Buchmeier MJ (e_1_3_3_3_2) 2007 Takagi T (e_1_3_3_49_2) 2012; 62 e_1_3_3_5_2 e_1_3_3_7_2 e_1_3_3_9_2 e_1_3_3_27_2 Centers for Disease Control and Prevention (CDC) (e_1_3_3_6_2) 2005 e_1_3_3_29_2 e_1_3_3_23_2 e_1_3_3_48_2 e_1_3_3_25_2 e_1_3_3_46_2 e_1_3_3_44_2 e_1_3_3_21_2 e_1_3_3_42_2 e_1_3_3_51_2 e_1_3_3_17_2 e_1_3_3_19_2 e_1_3_3_38_2 e_1_3_3_13_2 e_1_3_3_36_2 e_1_3_3_15_2 e_1_3_3_34_2 e_1_3_3_57_2 e_1_3_3_32_2 e_1_3_3_55_2 e_1_3_3_11_2 e_1_3_3_30_2 e_1_3_3_53_2 Jahrling PB (e_1_3_3_4_2) 1992; 116 Buchmeier M (e_1_3_3_2_2) 2013 e_1_3_3_8_2 e_1_3_3_28_2 e_1_3_3_24_2 e_1_3_3_47_2 e_1_3_3_26_2 e_1_3_3_45_2 e_1_3_3_20_2 e_1_3_3_43_2 e_1_3_3_22_2 e_1_3_3_41_2
References_xml	– ident: e_1_3_3_47_2 doi: 10.1128/JVI.07241-11 – ident: e_1_3_3_21_2 doi: 10.1038/nature05539 – ident: e_1_3_3_39_2 doi: 10.1128/JVI.00499-07 – ident: e_1_3_3_16_2 doi: 10.1099/vir.0.80473-0 – ident: e_1_3_3_28_2 doi: 10.1006/viro.2000.0357 – ident: e_1_3_3_51_2 doi: 10.1016/j.chom.2013.10.010 – ident: e_1_3_3_46_2 doi: 10.1128/JVI.01837-10 – ident: e_1_3_3_55_2 doi: 10.1038/nprot.2007.132 – ident: e_1_3_3_13_2 doi: 10.1128/JVI.00208-06 – ident: e_1_3_3_32_2 doi: 10.1074/jbc.M009613200 – ident: e_1_3_3_17_2 doi: 10.1128/JVI.77.19.10700-10705.2003 – ident: e_1_3_3_11_2 doi: 10.1038/sj.embor.7400002 – ident: e_1_3_3_7_2 doi: 10.1056/NEJMoa053240 – ident: e_1_3_3_18_2 doi: 10.1128/JVI.80.8.4191-4195.2006 – ident: e_1_3_3_31_2 doi: 10.1128/mBio.00180-12 – ident: e_1_3_3_36_2 doi: 10.1074/jbc.M312975200 – ident: e_1_3_3_38_2 doi: 10.1128/JVI.02779-06 – ident: e_1_3_3_19_2 doi: 10.1074/jbc.M302343200 – ident: e_1_3_3_52_2 doi: 10.1016/0042-6822(89)90610-7 – ident: e_1_3_3_35_2 doi: 10.1128/JVI.01481-07 – ident: e_1_3_3_30_2 doi: 10.1128/JVI.02759-06 – ident: e_1_3_3_5_2 doi: 10.1016/S0002-9394(00)00570-5 – ident: e_1_3_3_41_2 doi: 10.1016/j.virol.2010.10.011 – volume: 62 start-page: 185 year: 2012 ident: e_1_3_3_49_2 article-title: Genomic analysis and pathogenic characteristics of lymphocytic choriomeningitis virus strains isolated in Japan publication-title: Comp. Med. – ident: e_1_3_3_25_2 doi: 10.1099/vir.0.82950-0 – ident: e_1_3_3_9_2 doi: 10.1089/vbz.2011.0892 – ident: e_1_3_3_50_2 doi: 10.1073/pnas.1113643108 – start-page: 1792 volume-title: Fields virology year: 2007 ident: e_1_3_3_3_2 – ident: e_1_3_3_29_2 doi: 10.1074/jbc.M101638200 – ident: e_1_3_3_27_2 doi: 10.1128/JVI.02545-05 – start-page: 537 volume-title: MMWR Morb. Mortal. Wkly. Rep. year: 2005 ident: e_1_3_3_6_2 – ident: e_1_3_3_57_2 doi: 10.1016/0042-6822(88)90616-2 – ident: e_1_3_3_44_2 doi: 10.1186/1743-422X-5-161 – ident: e_1_3_3_34_2 doi: 10.1016/S0042-6822(03)00421-5 – ident: e_1_3_3_43_2 doi: 10.1016/j.virol.2012.10.038 – ident: e_1_3_3_48_2 doi: 10.1128/JVI.02410-08 – ident: e_1_3_3_56_2 doi: 10.1016/0042-6822(83)90135-6 – ident: e_1_3_3_53_2 doi: 10.1128/JVI.75.2.1061-1064.2001 – ident: e_1_3_3_8_2 doi: 10.1016/j.mib.2008.06.001 – ident: e_1_3_3_37_2 doi: 10.1016/j.virol.2006.08.048 – ident: e_1_3_3_54_2 doi: 10.1016/0378-1119(91)90434-D – ident: e_1_3_3_14_2 doi: 10.1073/pnas.221447598 – ident: e_1_3_3_33_2 doi: 10.1128/JVI.02146-06 – ident: e_1_3_3_40_2 doi: 10.1016/0042-6822(81)90137-9 – ident: e_1_3_3_15_2 doi: 10.1128/JVI.77.5.2866-2872.2003 – volume: 116 start-page: 486 year: 1992 ident: e_1_3_3_4_2 article-title: Lymphocytic choriomeningitis virus. A neglected pathogen of man publication-title: Arch. Pathol. Lab. Med. – ident: e_1_3_3_23_2 doi: 10.1126/science.1252480 – ident: e_1_3_3_42_2 doi: 10.1006/viro.1994.1057 – ident: e_1_3_3_12_2 doi: 10.1128/JVI.78.19.10783-10792.2004 – ident: e_1_3_3_26_2 doi: 10.1016/S0962-8924(98)01360-9 – ident: e_1_3_3_10_2 doi: 10.1128/jvi.52.3.897-904.1984 – ident: e_1_3_3_45_2 doi: 10.1016/j.febslet.2010.09.032 – start-page: 1283 volume-title: Fields virology year: 2013 ident: e_1_3_3_2_2 – ident: e_1_3_3_22_2 doi: 10.1126/scitranslmed.3006827 – ident: e_1_3_3_24_2 doi: 10.1006/viro.1995.1225 – ident: e_1_3_3_20_2 doi: 10.1126/science.282.5396.2079
SSID	ssj0000331830
Score	2.2906744
Snippet	The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and... ABSTRACT The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP,...
SourceID	doaj pubmedcentral proquest pubmed crossref
SourceType	Open Website Open Access Repository Aggregation Database Index Database Enrichment Source
StartPage	e02063
SubjectTerms	Amino acids Animals Antibodies biosynthesis Cell Line Cell Membrane - chemistry Cell Membrane - virology Cell membranes Confocal microscopy Endoplasmic reticulum Endosomes Enzymes fever Flow Cytometry Genomes Glycoproteins Glycoproteins - metabolism Golgi apparatus Hemorrhagic fever Humans Immunoprecipitation Infectivity Internalization Lymphocytic choriomeningitis mammarenavirus Lymphocytic choriomeningitis virus - physiology Maturation Membrane fusion Membrane trafficking Microscopy Microscopy, Confocal Molecular Biology Mutation pathogenicity pathogens Peptides pH effects plasma membrane polypeptides precipitin tests Protein Multimerization Protein Processing, Post-Translational Protein Sorting Signals Protein Subunits - metabolism Protein Transport Proteins Proteolysis receptors RNA polymerase rodents signal peptide Viral Structural Proteins - metabolism virion Virions Viruses
SummonAdditionalLinks	– databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1LixQxEA6yKHiR9d3uKhHEk-12nl193BVXRVgWVNiTofPShrFHpmcW999bSfcMM-Lj4rVTDUk9kq9I5StCngnuEDdYWQbZYoKilCutU6K0XoCvrG8Dj7nZRH12BhcXzflWq69UEzbSA4-KO2qFcuBt4j0PspEaJNi2cQJ0y5vo89M9RD1byVTeg0Xy1WpNqsnh6NtJN3-J2EiLksmdQyhz9f8OYP5aJ7l18Jzuk1sTYqTH40xvk2uhv0NujD0kr-6Sz8eL0LeX3WI1UESOdhboh-5L-uM8Faz4QN8NFFEefY82S8zbFPeKFQYyRbhK38yu3DxzNXQ9TXvDLPyg2-8z75FPp68_vnpbTk0TSqegWpagIIY6eohMO4t4wEaIVgoXpNVRtOCC11HZJnjm6ooF0aARdSV84ytutbhP9nqczENCQUtMt4CJulWSQQOR25pZxESVV47zgrxYa9G4iVE8NbaYmZxZcDBJ6SYrHVOMgjzfiH8fqTT-JHiSTLIRSgzY-QP6hZn8wvzLLwpyuDaomcJyMIhV08tZqHRBnm6GMaDSLUnbh_lqMKmDAKbNwNRfZGqZLkAZZwV5MPrIZrY8txzguIp6x3t2lrM70ndfM7G3xPyQQfXof6z_gNxEbDdxUh6SveViFR6T6-5y2Q2LJzlafgI8EBv4 priority: 102 providerName: Directory of Open Access Journals
Title	Arenavirus Stable Signal Peptide Is the Keystone Subunit for Glycoprotein Complex Organization
URI	https://www.ncbi.nlm.nih.gov/pubmed/25352624 https://www.proquest.com/docview/3263479806 https://www.proquest.com/docview/1618825815 https://www.proquest.com/docview/1746407121 https://pubmed.ncbi.nlm.nih.gov/PMC4217180 https://doaj.org/article/a35c8db8378e4946848ba9c386a29fd9
Volume	5
WOSCitedRecordID	wos000347073600035&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVAON databaseName: DOAJ Directory of Open Access Journals customDbUrl: eissn: 2150-7511 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000331830 issn: 2161-2129 databaseCode: DOA dateStart: 20100101 isFulltext: true titleUrlDefault: https://www.doaj.org/ providerName: Directory of Open Access Journals – providerCode: PRVPQU databaseName: Biological Science Database customDbUrl: eissn: 2150-7511 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000331830 issn: 2161-2129 databaseCode: M7P dateStart: 20100501 isFulltext: true titleUrlDefault: http://search.proquest.com/biologicalscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 2150-7511 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000331830 issn: 2161-2129 databaseCode: BENPR dateStart: 20100501 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: Public Health Database customDbUrl: eissn: 2150-7511 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000331830 issn: 2161-2129 databaseCode: 8C1 dateStart: 20100501 isFulltext: true titleUrlDefault: https://search.proquest.com/publichealth providerName: ProQuest – providerCode: PRVPQU databaseName: Publicly Available Content Database customDbUrl: eissn: 2150-7511 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000331830 issn: 2161-2129 databaseCode: PIMPY dateStart: 20100501 isFulltext: true titleUrlDefault: http://search.proquest.com/publiccontent providerName: ProQuest
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9QwELZoCxck3tBAWRkJcSI0sZ1kckJt1UKFWEU8pOVCFD9SIm2TNtmt6L9n7GRDF0EvXHJwJpKdGY-_GdvfEPKSM4W4QQrfiAIDlChSvlQR96XmoAOpC8NKV2wimU5hNkuzIeHWDccqVz7ROWrdKJsj30WYYS89QhC_PTv3bdUou7s6lNDYIFuWJYG7o3vZmGMJuLVYm2ZhCGx89NLpimaTwe6prJo3iJZi7odibVly7P1_g5x_npy8shQd3f3fQdwjdwYQSvd6q7lPbpj6AbnVl6W8fEi-77WmLi6qdtlRBKNybujn6sR-kdkzMNrQ444icKQf0AwsmTdF97NE30ARAdN380vVOPqHqqbW3czNT3r1yucj8vXo8MvBe3-ow-CrCIKFDxGUJik1lGGsJEIMWUIpBVdGyLjkBSij4zKSqdGhSoLQ8BTtIg64TnXAZMwfk80aO7NNKMQCIzgIeVJEIoQUSiaTUCLMCnSkGPPI65UacjWQlNtaGfPcBSsM8lP8GbnTGkYtHnk1ip_17Bz_Ety3Oh2FLKm2a2jak3yYo3nBIwVaWop9I1IRgwBZpIpDXLC01KlHdlZazYeZ3uW_VeqRF-NrnKN246WoTbPscluUACNxCKNrZBJh91TRjD3ypDeysbfMVTFgOIpkzfzWhrP-pq5-OK5wgSFnCMHT67v-jNy2oTfjPYXlDtlctEvznNxUF4uqaydkI5kBPuEgnJCt_cNp9mnishcTN-GwLTv-mH37BScsMoc
linkProvider	ProQuest
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Jb9QwFLZKAcGFfRkoYCTgRGi8JS8HhMpSOmoZVaJIPRHiJSXSNFMmM4X5U_xGnj3J0EHQWw9cYyeynbd8z35-HyFPBDeIG7SMnCwwQFHKRNooEWkrwMbaFo6XgWwiHQxgfz_bXSE_u7swPq2ys4nBUNuR8Xvk6wgz_KVHiJNXR98izxrlT1c7Co25WGy72XcM2ZqX_bf4f59yvvlu781W1LIKREZBPIlAQenS0kLJEqPRYeoSSi2FcVInpSjAOJuUSmfOMpPGzIkMZ5nEwmY25joR-N1z5DzCCA4hVXB3sacTC68hfluHI5CK0CtkXVlPDuuHuhq9QHSWiIjJJTcY2AL-BnH_zNQ84fo2r_5vi3aNXGlBNt2Ya8V1suLqG-TinHZzdpN83hi7ujiuxtOGItjWQ0c_Vgf-jV2f42Md7TcUgTHFQXtsjM1TPUXbRxHh0_fDmRmF8hZVTb05Hbof9OSV1lvk05lM7jZZrXEwdwmFRGKECkykhZIMMii5TplGGBlbZTjvkefdb89NW4Tdc4EM8xCMccgPcTHyICUYlfXIs0X3o3n1kX91fO1laNHJFw0PD0bjg7y1QXkhlAGrPYWAk5lMQIIuMiMgKXhW2qxH1jopyltL1uS_RahHHi-a0Qb5g6WidqNpk3vSBeAKmDqlTyr9mTHjrEfuzIV6MVoeWBo4ziJdEvel6Sy31NXXUAtdYkjNIL53-tAfkUtbex928p3-YPs-uYygty3WuUZWJ-Ope0AumONJ1YwfBoWm5MtZK8MvSwyM4A
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Arenavirus+stable+signal+peptide+is+the+keystone+subunit+for+glycoprotein+complex+organization&rft.jtitle=mBio&rft.au=Bederka%2C+Lydia+H&rft.au=Bonhomme%2C+Cyrille+J&rft.au=Ling%2C+Emily+L&rft.au=Buchmeier%2C+Michael+J&rft.date=2014-12-31&rft.issn=2150-7511&rft.eissn=2150-7511&rft.volume=5&rft.issue=6&rft.spage=e02063&rft_id=info:doi/10.1128%2FmBio.02063-14&rft.externalDBID=NO_FULL_TEXT
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2161-2129&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2161-2129&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2161-2129&client=summon