PySupercharge: a python algorithm for enabling ABC transporter bacterial secretion of all proteins through amino acid mutation

Background The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the...

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Published in:Microbial cell factories Vol. 23; no. 1; pp. 115 - 9
Main Authors: Kim, Yerin, Kim, Danny, Hieu, Nguyen-Mihn, Byun, Hyunjong, Ahn, Jung Hoon
Format: Journal Article
Language:English
Published: London BioMed Central 20.04.2024
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Abstract Background The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the ABC transporter after synthesis, a phenomenon we previously determined to be caused by an excessive positive charge in certain regions of their amino acid sequence. If such an excessive charge is removed, the secretion of any protein through ABC transporters becomes possible. Results In this study, we introduce ‘linear charge density’ as the criteria for possibility of protein secretion through ABC transporters and confirm that this criterion can be applied to various non-secretable proteins, such as SARS-CoV-2 spike proteins, botulinum toxin light chain, and human growth factors. Additionally, we develop a new algorithm, PySupercharge, that enables the secretion of proteins containing regions with high linear charge density. It selectively converts positively charged amino acids into negatively charged or neutral amino acids after linear charge density analysis to enable protein secretion through ABC transporters. Conclusions PySupercharge, which also minimizes functional/structural stability loss of the pre-mutation proteins through the use of sequence conservation data, is currently being operated on an accessible web server. We verified the efficacy of PySupercharge-driven protein supercharging by secreting various previously non-secretable proteins commonly used in research, and so suggest this tool for use in future research requiring effective protein production.
AbstractList Abstract Background The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the ABC transporter after synthesis, a phenomenon we previously determined to be caused by an excessive positive charge in certain regions of their amino acid sequence. If such an excessive charge is removed, the secretion of any protein through ABC transporters becomes possible. Results In this study, we introduce ‘linear charge density’ as the criteria for possibility of protein secretion through ABC transporters and confirm that this criterion can be applied to various non-secretable proteins, such as SARS-CoV-2 spike proteins, botulinum toxin light chain, and human growth factors. Additionally, we develop a new algorithm, PySupercharge, that enables the secretion of proteins containing regions with high linear charge density. It selectively converts positively charged amino acids into negatively charged or neutral amino acids after linear charge density analysis to enable protein secretion through ABC transporters. Conclusions PySupercharge, which also minimizes functional/structural stability loss of the pre-mutation proteins through the use of sequence conservation data, is currently being operated on an accessible web server. We verified the efficacy of PySupercharge-driven protein supercharging by secreting various previously non-secretable proteins commonly used in research, and so suggest this tool for use in future research requiring effective protein production.
The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the ABC transporter after synthesis, a phenomenon we previously determined to be caused by an excessive positive charge in certain regions of their amino acid sequence. If such an excessive charge is removed, the secretion of any protein through ABC transporters becomes possible.BACKGROUNDThe process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the ABC transporter after synthesis, a phenomenon we previously determined to be caused by an excessive positive charge in certain regions of their amino acid sequence. If such an excessive charge is removed, the secretion of any protein through ABC transporters becomes possible.In this study, we introduce 'linear charge density' as the criteria for possibility of protein secretion through ABC transporters and confirm that this criterion can be applied to various non-secretable proteins, such as SARS-CoV-2 spike proteins, botulinum toxin light chain, and human growth factors. Additionally, we develop a new algorithm, PySupercharge, that enables the secretion of proteins containing regions with high linear charge density. It selectively converts positively charged amino acids into negatively charged or neutral amino acids after linear charge density analysis to enable protein secretion through ABC transporters.RESULTSIn this study, we introduce 'linear charge density' as the criteria for possibility of protein secretion through ABC transporters and confirm that this criterion can be applied to various non-secretable proteins, such as SARS-CoV-2 spike proteins, botulinum toxin light chain, and human growth factors. Additionally, we develop a new algorithm, PySupercharge, that enables the secretion of proteins containing regions with high linear charge density. It selectively converts positively charged amino acids into negatively charged or neutral amino acids after linear charge density analysis to enable protein secretion through ABC transporters.PySupercharge, which also minimizes functional/structural stability loss of the pre-mutation proteins through the use of sequence conservation data, is currently being operated on an accessible web server. We verified the efficacy of PySupercharge-driven protein supercharging by secreting various previously non-secretable proteins commonly used in research, and so suggest this tool for use in future research requiring effective protein production.CONCLUSIONSPySupercharge, which also minimizes functional/structural stability loss of the pre-mutation proteins through the use of sequence conservation data, is currently being operated on an accessible web server. We verified the efficacy of PySupercharge-driven protein supercharging by secreting various previously non-secretable proteins commonly used in research, and so suggest this tool for use in future research requiring effective protein production.
The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the ABC transporter after synthesis, a phenomenon we previously determined to be caused by an excessive positive charge in certain regions of their amino acid sequence. If such an excessive charge is removed, the secretion of any protein through ABC transporters becomes possible. In this study, we introduce 'linear charge density' as the criteria for possibility of protein secretion through ABC transporters and confirm that this criterion can be applied to various non-secretable proteins, such as SARS-CoV-2 spike proteins, botulinum toxin light chain, and human growth factors. Additionally, we develop a new algorithm, PySupercharge, that enables the secretion of proteins containing regions with high linear charge density. It selectively converts positively charged amino acids into negatively charged or neutral amino acids after linear charge density analysis to enable protein secretion through ABC transporters. PySupercharge, which also minimizes functional/structural stability loss of the pre-mutation proteins through the use of sequence conservation data, is currently being operated on an accessible web server. We verified the efficacy of PySupercharge-driven protein supercharging by secreting various previously non-secretable proteins commonly used in research, and so suggest this tool for use in future research requiring effective protein production.
The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the ABC transporter after synthesis, a phenomenon we previously determined to be caused by an excessive positive charge in certain regions of their amino acid sequence. If such an excessive charge is removed, the secretion of any protein through ABC transporters becomes possible. In this study, we introduce 'linear charge density' as the criteria for possibility of protein secretion through ABC transporters and confirm that this criterion can be applied to various non-secretable proteins, such as SARS-CoV-2 spike proteins, botulinum toxin light chain, and human growth factors. Additionally, we develop a new algorithm, PySupercharge, that enables the secretion of proteins containing regions with high linear charge density. It selectively converts positively charged amino acids into negatively charged or neutral amino acids after linear charge density analysis to enable protein secretion through ABC transporters. PySupercharge, which also minimizes functional/structural stability loss of the pre-mutation proteins through the use of sequence conservation data, is currently being operated on an accessible web server. We verified the efficacy of PySupercharge-driven protein supercharging by secreting various previously non-secretable proteins commonly used in research, and so suggest this tool for use in future research requiring effective protein production.
Background The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the ABC transporter after synthesis, a phenomenon we previously determined to be caused by an excessive positive charge in certain regions of their amino acid sequence. If such an excessive charge is removed, the secretion of any protein through ABC transporters becomes possible. Results In this study, we introduce 'linear charge density' as the criteria for possibility of protein secretion through ABC transporters and confirm that this criterion can be applied to various non-secretable proteins, such as SARS-CoV-2 spike proteins, botulinum toxin light chain, and human growth factors. Additionally, we develop a new algorithm, PySupercharge, that enables the secretion of proteins containing regions with high linear charge density. It selectively converts positively charged amino acids into negatively charged or neutral amino acids after linear charge density analysis to enable protein secretion through ABC transporters. Conclusions PySupercharge, which also minimizes functional/structural stability loss of the pre-mutation proteins through the use of sequence conservation data, is currently being operated on an accessible web server. We verified the efficacy of PySupercharge-driven protein supercharging by secreting various previously non-secretable proteins commonly used in research, and so suggest this tool for use in future research requiring effective protein production. Keywords: Python Algorithm, Supercharging, Protein production, Secretion, ABC Transporter
Background The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively researched and used due to its high protein production capacity and efficiency. However, some proteins are unable to pass through the ABC transporter after synthesis, a phenomenon we previously determined to be caused by an excessive positive charge in certain regions of their amino acid sequence. If such an excessive charge is removed, the secretion of any protein through ABC transporters becomes possible. Results In this study, we introduce ‘linear charge density’ as the criteria for possibility of protein secretion through ABC transporters and confirm that this criterion can be applied to various non-secretable proteins, such as SARS-CoV-2 spike proteins, botulinum toxin light chain, and human growth factors. Additionally, we develop a new algorithm, PySupercharge, that enables the secretion of proteins containing regions with high linear charge density. It selectively converts positively charged amino acids into negatively charged or neutral amino acids after linear charge density analysis to enable protein secretion through ABC transporters. Conclusions PySupercharge, which also minimizes functional/structural stability loss of the pre-mutation proteins through the use of sequence conservation data, is currently being operated on an accessible web server. We verified the efficacy of PySupercharge-driven protein supercharging by secreting various previously non-secretable proteins commonly used in research, and so suggest this tool for use in future research requiring effective protein production.
ArticleNumber 115
Audience Academic
Author Kim, Yerin
Byun, Hyunjong
Ahn, Jung Hoon
Kim, Danny
Hieu, Nguyen-Mihn
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10.1038/s41586-021-03819-2
10.1186/s12934-018-1041-5
10.1093/nar/gkq399
10.1016/S0005-2736(99)00158-3
10.1002/ijch.201200096
10.3390/biomedicines9060679
10.1021/ja071641y
10.3390/microorganisms8020239
10.1128/AEM.03514-14
10.1002/btpr.2911
10.1002/j.1460-2075.1996.tb00967.x
10.1371/journal.pone.0064363
10.1128/AEM.01163-17
10.1016/j.biotechadv.2011.09.013
10.1021/bi9004107
10.1074/jbc.M110.173658
10.1128/AEM.02476-12
10.1093/nar/gkw408
10.1002/(sici)1097-0320(19990101)35:1<55::aid-cyto8>3.0.co;2-2
10.1186/1475-2859-11-601475-2859-11-60
10.1128/JB.181.6.1847-1852.1999
10.1016/j.bbamcr.2013.09
10.1186/1475-2859-8-11
10.1186/s12934-018-0901-3
10.3389/fmicb.2014.00172
10.1080/09687860500042013
10.1002/elsc.201700200
10.1074/jbc.M117.786749
10.1111/j.1574-6976.2012.00327.x
10.1159/000083259
10.3390/ijms23126700
10.1186/1475-2859-4-1
10.1016/B978-0-12-396962-0.00012-4
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Keywords Python Algorithm
Supercharging
Protein production
Secretion
ABC Transporter
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References R Chen (2342_CR4) 2012; 30
N Ihling (2342_CR10) 2020; 36
R Freudl (2342_CR8) 2018; 17
KM Slade (2342_CR7) 2009; 48
D Novo (2342_CR26) 1999; 35
M Son (2342_CR19) 2012; 78
BS Der (2342_CR28) 2013; 8
CW Chung (2342_CR22) 2009; 8
H Byun (2342_CR1) 2017
Y Park (2342_CR17) 2012; 11
D Dressler (2342_CR33) 2005; 53
GRM Kleiner-Grote (2342_CR9) 2018; 18
J Ryu (2342_CR18) 2015; 81
G Celniker (2342_CR31) 2013; 53
2342_CR25
2342_CR24
S Letoffe (2342_CR13) 1996; 15
RE Dalbey (2342_CR20) 2012; 36
2342_CR32
2342_CR11
J Young (2342_CR14) 1999; 1461
HP Sorensen (2342_CR5) 2005; 4
MS Lawrence (2342_CR27) 2007; 129
PJ Bakkes (2342_CR23) 2010; 285
JH Ahn (2342_CR15) 1999; 181
GL Rosano (2342_CR6) 2014; 5
S Thomas (2342_CR12) 2014; 1843
LA Burdette (2342_CR21) 2018; 17
H Ashkenazy (2342_CR30) 2010; 38
DB Thompson (2342_CR34) 2012; 503
H Ashkenazy (2342_CR29) 2016; 44
B-U Fabia (2342_CR2) 2021; 9
IB Holland (2342_CR3) 2005; 22
2342_CR16
References_xml – ident: 2342_CR11
  doi: 10.1128/microbiolspec.VMBF-0012-2015
– ident: 2342_CR32
  doi: 10.1038/s41586-021-03819-2
– volume: 17
  start-page: 196
  issue: 1
  year: 2018
  ident: 2342_CR21
  publication-title: Microb Cell Fact
  doi: 10.1186/s12934-018-1041-5
– volume: 38
  start-page: W529
  issue: suppl2
  year: 2010
  ident: 2342_CR30
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/gkq399
– volume: 1461
  start-page: 177
  issue: 2
  year: 1999
  ident: 2342_CR14
  publication-title: Biochim et Biophys Acta (BBA)-Biomembranes
  doi: 10.1016/S0005-2736(99)00158-3
– volume: 53
  start-page: 199
  issue: 3–4
  year: 2013
  ident: 2342_CR31
  publication-title: Isr J Chem
  doi: 10.1002/ijch.201200096
– volume: 9
  start-page: 679
  issue: 6
  year: 2021
  ident: 2342_CR2
  publication-title: Biomedicines
  doi: 10.3390/biomedicines9060679
– volume: 129
  start-page: 10110
  issue: 33
  year: 2007
  ident: 2342_CR27
  publication-title: J Am Chem Soc
  doi: 10.1021/ja071641y
– ident: 2342_CR16
  doi: 10.3390/microorganisms8020239
– volume: 81
  start-page: 1744
  issue: 5
  year: 2015
  ident: 2342_CR18
  publication-title: Appl Environ Microbiol
  doi: 10.1128/AEM.03514-14
– volume: 36
  start-page: e2911
  issue: 2
  year: 2020
  ident: 2342_CR10
  publication-title: Biotechnol Prog
  doi: 10.1002/btpr.2911
– volume: 15
  start-page: 5804
  issue: 21
  year: 1996
  ident: 2342_CR13
  publication-title: EMBO J
  doi: 10.1002/j.1460-2075.1996.tb00967.x
– volume: 8
  start-page: e64363
  issue: 5
  year: 2013
  ident: 2342_CR28
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0064363
– ident: 2342_CR24
  doi: 10.1128/AEM.01163-17
– volume: 30
  start-page: 1102
  issue: 5
  year: 2012
  ident: 2342_CR4
  publication-title: Biotechnol Adv
  doi: 10.1016/j.biotechadv.2011.09.013
– volume: 48
  start-page: 5083
  issue: 23
  year: 2009
  ident: 2342_CR7
  publication-title: Biochemistry
  doi: 10.1021/bi9004107
– volume: 285
  start-page: 40573
  issue: 52
  year: 2010
  ident: 2342_CR23
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M110.173658
– volume: 78
  start-page: 8454
  issue: 23
  year: 2012
  ident: 2342_CR19
  publication-title: Appl Environ Microbiol
  doi: 10.1128/AEM.02476-12
– volume: 44
  start-page: W344
  issue: W1
  year: 2016
  ident: 2342_CR29
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/gkw408
– volume: 35
  start-page: 55
  issue: 1
  year: 1999
  ident: 2342_CR26
  publication-title: Cytometry
  doi: 10.1002/(sici)1097-0320(19990101)35:1<55::aid-cyto8>3.0.co;2-2
– volume: 11
  start-page: 60
  year: 2012
  ident: 2342_CR17
  publication-title: Microb Cell Fact
  doi: 10.1186/1475-2859-11-601475-2859-11-60
– volume: 181
  start-page: 1847
  issue: 6
  year: 1999
  ident: 2342_CR15
  publication-title: J Bacteriol
  doi: 10.1128/JB.181.6.1847-1852.1999
– volume: 1843
  start-page: 1629
  issue: 8
  year: 2014
  ident: 2342_CR12
  publication-title: Biochim Biophys Acta
  doi: 10.1016/j.bbamcr.2013.09
– volume: 8
  start-page: 11
  issue: 1
  year: 2009
  ident: 2342_CR22
  publication-title: Microb Cell Fact
  doi: 10.1186/1475-2859-8-11
– volume: 17
  start-page: 52
  issue: 1
  year: 2018
  ident: 2342_CR8
  publication-title: Microb Cell Fact
  doi: 10.1186/s12934-018-0901-3
– volume: 5
  start-page: 172
  year: 2014
  ident: 2342_CR6
  publication-title: Front Microbiol
  doi: 10.3389/fmicb.2014.00172
– volume: 22
  start-page: 29
  issue: 1–2
  year: 2005
  ident: 2342_CR3
  publication-title: Mol Membr Biol
  doi: 10.1080/09687860500042013
– volume: 18
  start-page: 532
  issue: 8
  year: 2018
  ident: 2342_CR9
  publication-title: Eng Life Sci
  doi: 10.1002/elsc.201700200
– year: 2017
  ident: 2342_CR1
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M117.786749
– volume: 36
  start-page: 1023
  issue: 6
  year: 2012
  ident: 2342_CR20
  publication-title: FEMS Microbiol Rev
  doi: 10.1111/j.1574-6976.2012.00327.x
– volume: 53
  start-page: 3
  issue: 1
  year: 2005
  ident: 2342_CR33
  publication-title: Eur Neurol
  doi: 10.1159/000083259
– ident: 2342_CR25
  doi: 10.3390/ijms23126700
– volume: 4
  start-page: 1
  issue: 1
  year: 2005
  ident: 2342_CR5
  publication-title: Microb Cell Fact
  doi: 10.1186/1475-2859-4-1
– volume: 503
  start-page: 293
  year: 2012
  ident: 2342_CR34
  publication-title: Methods Enzymol
  doi: 10.1016/B978-0-12-396962-0.00012-4
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Snippet Background The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been...
The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been actively...
Background The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that has been...
Abstract Background The process of producing proteins in bacterial systems and secreting them through ATP-binding cassette (ABC) transporters is an area that...
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SubjectTerms ABC Transporter
Algorithms
Amino acids
Analysis
Applied Microbiology
Biotechnology
Chemistry
Chemistry and Materials Science
Enzymology
Genetic Engineering
Health aspects
Information management
Methodology
Microbial Genetics and Genomics
Microbiology
Protein production
Proteins
Python (Programming language)
Python Algorithm
Secretion
Supercharging
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Title PySupercharge: a python algorithm for enabling ABC transporter bacterial secretion of all proteins through amino acid mutation
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