Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies

The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated ancestor (putative naive B cell rec...

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Veröffentlicht in:	PLoS pathogens Jg. 7; H. 9; S. e1002200
Hauptverfasser:	Ma, Ben-Jiang, Alam, S. Munir, Go, Eden P., Lu, Xiaozhi, Desaire, Heather, Tomaras, Georgia D., Bowman, Cindy, Sutherland, Laura L., Scearce, Richard M., Santra, Sampa, Letvin, Norman L., Kepler, Thomas B., Liao, Hua-Xin, Haynes, Barton F.
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States Public Library of Science 01.09.2011 Public Library of Science (PLoS)
Schlagworte:	Acquired immune deficiency syndrome AIDS Animals Antibodies, Monoclonal - immunology Antibodies, Neutralizing - immunology Antigen-antibody reactions B-Lymphocytes - immunology Biology env Gene Products, Human Immunodeficiency Virus - chemistry env Gene Products, Human Immunodeficiency Virus - immunology Epitopes - immunology Experiments Flow cytometry Glycosylation HIV (Viruses) HIV antibodies HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp41 - immunology HIV-1 - immunology Humans Hypotheses Immunization Immunogenicity Immunology Macaca mulatta - immunology Medicine Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism Peptides Physiological aspects Proteins Vaccines United States
ISSN:	1553-7374, 1553-7366, 1553-7374
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Abstract	The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated ancestor (putative naive B cell receptor) antibody reactivity with HIV-1 envelope. We have studied the effect of partial deglycosylation under non-denaturing (native) conditions on gp140 Env antigenicity for MPER neutralizing antibodies and their reverted unmutated ancestor antibodies. We found that native deglycosylation of clade B JRFL gp140 as well as group M consensus gp140 Env CON-S selectively increased the reactivity of Env with the broad neutralizing human mAbs, 2F5 and 4E10. Whereas fully glycosylated gp140 Env either did not bind (JRFL), or weakly bound (CON-S), 2F5 and 4E10 reverted unmutated ancestors, natively deglycosylated JRFL and CON-S gp140 Envs did bind well to these putative mimics of naive B cell receptors. These data predict that partially deglycoslated Env would bind better than fully glycosylated Env to gp41-specific naïve B cells with improved immunogenicity. In this regard, immunization of rhesus macaques demonstrated enhanced immunogenicity of the 2F5 MPER epitope on deglyosylated JRFL gp140 compared to glycosylated JRFL gp140. Thus, the lack of 2F5 and 4E10 reverted unmutated ancestor binding to gp140 Env may not always be due to lack of unmutated ancestor antibody reactivity with gp41 peptide epitopes, but rather, may be due to glycan interference of binding of unmutated ancestor antibodies of broad neutralizing mAb to Env gp41.
AbstractList	The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated ancestor (putative naive B cell receptor) antibody reactivity with HIV-1 envelope. We have studied the effect of partial deglycosylation under non-denaturing (native) conditions on gp140 Env antigenicity for MPER neutralizing antibodies and their reverted unmutated ancestor antibodies. We found that native deglycosylation of clade B JRFL gp140 as well as group M consensus gp140 Env CON-S selectively increased the reactivity of Env with the broad neutralizing human mAbs, 2F5 and 4E10. Whereas fully glycosylated gp140 Env either did not bind (JRFL), or weakly bound (CON-S), 2F5 and 4E10 reverted unmutated ancestors, natively deglycosylated JRFL and CON-S gp140 Envs did bind well to these putative mimics of naive B cell receptors. These data predict that partially deglycoslated Env would bind better than fully glycosylated Env to gp41-specific naïve B cells with improved immunogenicity. In this regard, immunization of rhesus macaques demonstrated enhanced immunogenicity of the 2F5 MPER epitope on deglyosylated JRFL gp140 compared to glycosylated JRFL gp140. Thus, the lack of 2F5 and 4E10 reverted unmutated ancestor binding to gp140 Env may not always be due to lack of unmutated ancestor antibody reactivity with gp41 peptide epitopes, but rather, may be due to glycan interference of binding of unmutated ancestor antibodies of broad neutralizing mAb to Env gp41. The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated ancestor (putative naive B cell receptor) antibody reactivity with HIV-1 envelope. We have studied the effect of partial deglycosylation under non-denaturing (native) conditions on gp140 Env antigenicity for MPER neutralizing antibodies and their reverted unmutated ancestor antibodies. We found that native deglycosylation of clade B JRFL gp140 as well as group M consensus gp140 Env CON-S selectively increased the reactivity of Env with the broad neutralizing human mAbs, 2F5 and 4E10. Whereas fully glycosylated gp140 Env either did not bind (JRFL), or weakly bound (CON-S), 2F5 and 4E10 reverted unmutated ancestors, natively deglycosylated JRFL and CON-S gp140 Envs did bind well to these putative mimics of naive B cell receptors. These data predict that partially deglycoslated Env would bind better than fully glycosylated Env to gp41-specific naïve B cells with improved immunogenicity. In this regard, immunization of rhesus macaques demonstrated enhanced immunogenicity of the 2F5 MPER epitope on deglyosylated JRFL gp140 compared to glycosylated JRFL gp140. Thus, the lack of 2F5 and 4E10 reverted unmutated ancestor binding to gp140 Env may not always be due to lack of unmutated ancestor antibody reactivity with gp41 peptide epitopes, but rather, may be due to glycan interference of binding of unmutated ancestor antibodies of broad neutralizing mAb to Env gp41. Critical to the design of an effective HIV-1 vaccine that will induce long-lasting broadly neutralizing antibodies is to understand why broad neutralizing antibodies are not induced. One hypothesis is that there are “holes” in the naïve B cell repertoires for unmutated B cell receptors that can bind to HIV-1 envelope (Env) neutralizing epitopes. In this paper, we test this hypothesis for the rare HIV-1 envelope gp41 broad neutralizing monoclonal antibodes (mAbs), called 2F5 and 4E10, and show that indeed, fully glycosylated Env does not bind to inferred unmutated ancestor antibodies (mimics of naïve B cell receptors) of mAbs 2F5 and 4E10, but that partially deglycosylated Envs that have had glycans removed under non-denaturing conditions, did bind to 2F5 and 4E10 unmutated ancestor antibodies. Thus, rather than there being a lack of existence of germline B cell receptors for gp41 broad neutralizing antibodies, one impediment to induction of gp41 broad neutralizing antibodies may be glycan interference with unmutated antibody binding to gp41 envelope. The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated ancestor (putative naive B cell receptor) antibody reactivity with HIV-1 envelope. We have studied the effect of partial deglycosylation under non-denaturing (native) conditions on gp140 Env antigenicity for MPER neutralizing antibodies and their reverted unmutated ancestor antibodies. We found that native deglycosylation of clade B JRFL gp140 as well as group M consensus gp140 Env CON-S selectively increased the reactivity of Env with the broad neutralizing human mAbs, 2F5 and 4E10. Whereas fully glycosylated gp140 Env either did not bind (JRFL), or weakly bound (CON-S), 2F5 and 4E10 reverted unmutated ancestors, natively deglycosylated JRFL and CON-S gp140 Envs did bind well to these putative mimics of naive B cell receptors. These data predict that partially deglycoslated Env would bind better than fully glycosylated Env to gp41-specific nai've B cells with improved immunogenicity. In this regard, immunization of rhesus macaques demonstrated enhanced immunogenicity of the 2F5 MPER epitope on deglyosylated JRFL gp140 compared to glycosylated JRFL gp140. Thus, the lack of 2F5 and 4E10 reverted unmutated ancestor binding to gp140 Env may not always be due to lack of unmutated ancestor antibody reactivity with gp41 peptide epitopes, but rather, may be due to glycan interference of binding of unmutated ancestor antibodies of broad neutralizing mAb to Env gp41. The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated ancestor (putative naive B cell receptor) antibody reactivity with HIV-1 envelope. We have studied the effect of partial deglycosylation under non-denaturing (native) conditions on gp140 Env antigenicity for MPER neutralizing antibodies and their reverted unmutated ancestor antibodies. We found that native deglycosylation of clade B JRFL gp140 as well as group M consensus gp140 Env CON-S selectively increased the reactivity of Env with the broad neutralizing human mAbs, 2F5 and 4E10. Whereas fully glycosylated gp140 Env either did not bind (JRFL), or weakly bound (CON-S), 2F5 and 4E10 reverted unmutated ancestors, natively deglycosylated JRFL and CON-S gp140 Envs did bind well to these putative mimics of naive B cell receptors. These data predict that partially deglycoslated Env would bind better than fully glycosylated Env to gp41-specific naïve B cells with improved immunogenicity. In this regard, immunization of rhesus macaques demonstrated enhanced immunogenicity of the 2F5 MPER epitope on deglyosylated JRFL gp140 compared to glycosylated JRFL gp140. Thus, the lack of 2F5 and 4E10 reverted unmutated ancestor binding to gp140 Env may not always be due to lack of unmutated ancestor antibody reactivity with gp41 peptide epitopes, but rather, may be due to glycan interference of binding of unmutated ancestor antibodies of broad neutralizing mAb to Env gp41. The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated ancestor (putative naive B cell receptor) antibody reactivity with HIV-1 envelope. We have studied the effect of partial deglycosylation under non-denaturing (native) conditions on gp140 Env antigenicity for MPER neutralizing antibodies and their reverted unmutated ancestor antibodies. We found that native deglycosylation of clade B JRFL gp140 as well as group M consensus gp140 Env CON-S selectively increased the reactivity of Env with the broad neutralizing human mAbs, 2F5 and 4E10. Whereas fully glycosylated gp140 Env either did not bind (JRFL), or weakly bound (CON-S), 2F5 and 4E10 reverted unmutated ancestors, natively deglycosylated JRFL and CON-S gp140 Envs did bind well to these putative mimics of naive B cell receptors. These data predict that partially deglycoslated Env would bind better than fully glycosylated Env to gp41-specific naïve B cells with improved immunogenicity. In this regard, immunization of rhesus macaques demonstrated enhanced immunogenicity of the 2F5 MPER epitope on deglyosylated JRFL gp140 compared to glycosylated JRFL gp140. Thus, the lack of 2F5 and 4E10 reverted unmutated ancestor binding to gp140 Env may not always be due to lack of unmutated ancestor antibody reactivity with gp41 peptide epitopes, but rather, may be due to glycan interference of binding of unmutated ancestor antibodies of broad neutralizing mAb to Env gp41.The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated ancestor (putative naive B cell receptor) antibody reactivity with HIV-1 envelope. We have studied the effect of partial deglycosylation under non-denaturing (native) conditions on gp140 Env antigenicity for MPER neutralizing antibodies and their reverted unmutated ancestor antibodies. We found that native deglycosylation of clade B JRFL gp140 as well as group M consensus gp140 Env CON-S selectively increased the reactivity of Env with the broad neutralizing human mAbs, 2F5 and 4E10. Whereas fully glycosylated gp140 Env either did not bind (JRFL), or weakly bound (CON-S), 2F5 and 4E10 reverted unmutated ancestors, natively deglycosylated JRFL and CON-S gp140 Envs did bind well to these putative mimics of naive B cell receptors. These data predict that partially deglycoslated Env would bind better than fully glycosylated Env to gp41-specific naïve B cells with improved immunogenicity. In this regard, immunization of rhesus macaques demonstrated enhanced immunogenicity of the 2F5 MPER epitope on deglyosylated JRFL gp140 compared to glycosylated JRFL gp140. Thus, the lack of 2F5 and 4E10 reverted unmutated ancestor binding to gp140 Env may not always be due to lack of unmutated ancestor antibody reactivity with gp41 peptide epitopes, but rather, may be due to glycan interference of binding of unmutated ancestor antibodies of broad neutralizing mAb to Env gp41.
Audience	Academic
Author	Sutherland, Laura L. Lu, Xiaozhi Kepler, Thomas B. Tomaras, Georgia D. Scearce, Richard M. Desaire, Heather Alam, S. Munir Santra, Sampa Go, Eden P. Letvin, Norman L. Bowman, Cindy Liao, Hua-Xin Ma, Ben-Jiang Haynes, Barton F.
AuthorAffiliation	1 Duke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, United States of America 5 Deparment of Surgery, Duke University School of Medicine, Durham, North Carolina, United States of America University of Zurich, Switzerland 6 Center for Computational Immunology, Duke University School of Medicine, Durham, North Carolina, United States of America 2 Department of Medicine, Duke University School of Medicine, Durham, North Carolina, United States of America 3 Department of Chemistry, University of Kansas, Lawrence, Kansas, United States of America 4 Department of Immunology, Duke University School of Medicine, Durham, North Carolina, United States of America 7 Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, United States of America
AuthorAffiliation_xml	– name: 2 Department of Medicine, Duke University School of Medicine, Durham, North Carolina, United States of America – name: 6 Center for Computational Immunology, Duke University School of Medicine, Durham, North Carolina, United States of America – name: 7 Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, United States of America – name: 5 Deparment of Surgery, Duke University School of Medicine, Durham, North Carolina, United States of America – name: University of Zurich, Switzerland – name: 1 Duke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, United States of America – name: 4 Department of Immunology, Duke University School of Medicine, Durham, North Carolina, United States of America – name: 3 Department of Chemistry, University of Kansas, Lawrence, Kansas, United States of America
Author_xml	– sequence: 1 givenname: Ben-Jiang surname: Ma fullname: Ma, Ben-Jiang – sequence: 2 givenname: S. Munir surname: Alam fullname: Alam, S. Munir – sequence: 3 givenname: Eden P. surname: Go fullname: Go, Eden P. – sequence: 4 givenname: Xiaozhi surname: Lu fullname: Lu, Xiaozhi – sequence: 5 givenname: Heather surname: Desaire fullname: Desaire, Heather – sequence: 6 givenname: Georgia D. surname: Tomaras fullname: Tomaras, Georgia D. – sequence: 7 givenname: Cindy surname: Bowman fullname: Bowman, Cindy – sequence: 8 givenname: Laura L. surname: Sutherland fullname: Sutherland, Laura L. – sequence: 9 givenname: Richard M. surname: Scearce fullname: Scearce, Richard M. – sequence: 10 givenname: Sampa surname: Santra fullname: Santra, Sampa – sequence: 11 givenname: Norman L. surname: Letvin fullname: Letvin, Norman L. – sequence: 12 givenname: Thomas B. surname: Kepler fullname: Kepler, Thomas B. – sequence: 13 givenname: Hua-Xin surname: Liao fullname: Liao, Hua-Xin – sequence: 14 givenname: Barton F. surname: Haynes fullname: Haynes, Barton F.
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/21909262$$D View this record in MEDLINE/PubMed
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ContentType	Journal Article
Copyright	COPYRIGHT 2011 Public Library of Science 2011 Ma et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Ma B-J, Alam SM, Go EP, Lu X, Desaire H, et al. (2011) Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies. PLoS Pathog 7(9): e1002200. doi:10.1371/journal.ppat.1002200 Ma et al. 2011
Copyright_xml	– notice: COPYRIGHT 2011 Public Library of Science – notice: 2011 Ma et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Ma B-J, Alam SM, Go EP, Lu X, Desaire H, et al. (2011) Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies. PLoS Pathog 7(9): e1002200. doi:10.1371/journal.ppat.1002200 – notice: Ma et al. 2011
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DocumentTitleAlternate	Deglycosylation of HIV-1 Env Enhances Antigenicity
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Conceived and designed the experiments: BFH HXL SMA NLL HD. Performed the experiments: BJM SMA EPG XZL CB LLS RMS SS GDT. Analyzed the data: BJM SMA HD TBK NLL HXL BFH. Contributed reagents/materials/analysis tools: BJM TBK HXL. Wrote the paper: HXL BJM BFH.
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Snippet	The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies.... The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing...
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SubjectTerms	Acquired immune deficiency syndrome AIDS Animals Antibodies, Monoclonal - immunology Antibodies, Neutralizing - immunology Antigen-antibody reactions B-Lymphocytes - immunology Biology env Gene Products, Human Immunodeficiency Virus - chemistry env Gene Products, Human Immunodeficiency Virus - immunology Epitopes - immunology Experiments Flow cytometry Glycosylation HIV (Viruses) HIV antibodies HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp41 - immunology HIV-1 - immunology Humans Hypotheses Immunization Immunogenicity Immunology Macaca mulatta - immunology Medicine Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism Peptides Physiological aspects Proteins Vaccines
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Title	Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies
URI	https://www.ncbi.nlm.nih.gov/pubmed/21909262 https://www.proquest.com/docview/1289082588 https://www.proquest.com/docview/889175761 https://pubmed.ncbi.nlm.nih.gov/PMC3164629 https://doaj.org/article/49a76dd39d4b4a07a1ec1488d4b6ba89 http://dx.doi.org/10.1371/journal.ppat.1002200
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