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HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments
BACKGROUND: N-linked glycosylation is a major mechanism for minimizing virus neutralizing antibody response and is present on the Human Immunodeficiency Virus (HIV) envelope glycoprotein. Although it is known that glycosylation changes can dramatically influence virus recognition by the host antibod...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2265691/ https://www.ncbi.nlm.nih.gov/pubmed/18215327 http://dx.doi.org/10.1186/1743-422X-5-14 |
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author | Ho, Yung Shwen Abecasis, Ana B Theys, Kristof Deforche, Koen Dwyer, Dominic E Charleston, Michael Vandamme, Anne Mieke Saksena, Nitin K |
author_facet | Ho, Yung Shwen Abecasis, Ana B Theys, Kristof Deforche, Koen Dwyer, Dominic E Charleston, Michael Vandamme, Anne Mieke Saksena, Nitin K |
author_sort | Ho, Yung Shwen |
collection | PubMed |
description | BACKGROUND: N-linked glycosylation is a major mechanism for minimizing virus neutralizing antibody response and is present on the Human Immunodeficiency Virus (HIV) envelope glycoprotein. Although it is known that glycosylation changes can dramatically influence virus recognition by the host antibody, the actual contribution of compartmental differences in N-linked glycosylation patterns remains unclear. METHODOLOGY AND PRINCIPAL FINDINGS: We amplified the env gp120 C2-V5 region and analyzed 305 clones derived from plasma and other compartments from 15 HIV-1 patients. Bioinformatics and Bayesian network analyses were used to examine N-linked glycosylation differences between compartments. We found evidence for cellspecific single amino acid changes particular to monocytes, and significant variation was found in the total number of N-linked glycosylation sites between patients. Further, significant differences in the number of glycosylation sites were observed between plasma and cellular compartments. Bayesian network analyses showed an interdependency between N-linked glycosylation sites found in our study, which may have immense functional relevance. CONCLUSION: Our analyses have identified single cell/compartment-specific amino acid changes and differences in N-linked glycosylation patterns between plasma and diverse blood leukocytes. Bayesian network analyses showed associations inferring alternative glycosylation pathways. We believe that these studies will provide crucial insights into the host immune response and its ability in controlling HIV replication in vivo. These findings could also have relevance in shielding and evasion of HIV-1 from neutralizing antibodies. |
format | Text |
id | pubmed-2265691 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-22656912008-03-08 HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments Ho, Yung Shwen Abecasis, Ana B Theys, Kristof Deforche, Koen Dwyer, Dominic E Charleston, Michael Vandamme, Anne Mieke Saksena, Nitin K Virol J Research BACKGROUND: N-linked glycosylation is a major mechanism for minimizing virus neutralizing antibody response and is present on the Human Immunodeficiency Virus (HIV) envelope glycoprotein. Although it is known that glycosylation changes can dramatically influence virus recognition by the host antibody, the actual contribution of compartmental differences in N-linked glycosylation patterns remains unclear. METHODOLOGY AND PRINCIPAL FINDINGS: We amplified the env gp120 C2-V5 region and analyzed 305 clones derived from plasma and other compartments from 15 HIV-1 patients. Bioinformatics and Bayesian network analyses were used to examine N-linked glycosylation differences between compartments. We found evidence for cellspecific single amino acid changes particular to monocytes, and significant variation was found in the total number of N-linked glycosylation sites between patients. Further, significant differences in the number of glycosylation sites were observed between plasma and cellular compartments. Bayesian network analyses showed an interdependency between N-linked glycosylation sites found in our study, which may have immense functional relevance. CONCLUSION: Our analyses have identified single cell/compartment-specific amino acid changes and differences in N-linked glycosylation patterns between plasma and diverse blood leukocytes. Bayesian network analyses showed associations inferring alternative glycosylation pathways. We believe that these studies will provide crucial insights into the host immune response and its ability in controlling HIV replication in vivo. These findings could also have relevance in shielding and evasion of HIV-1 from neutralizing antibodies. BioMed Central 2008-01-23 /pmc/articles/PMC2265691/ /pubmed/18215327 http://dx.doi.org/10.1186/1743-422X-5-14 Text en Copyright © 2008 Ho et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Ho, Yung Shwen Abecasis, Ana B Theys, Kristof Deforche, Koen Dwyer, Dominic E Charleston, Michael Vandamme, Anne Mieke Saksena, Nitin K HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments |
title | HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments |
title_full | HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments |
title_fullStr | HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments |
title_full_unstemmed | HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments |
title_short | HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments |
title_sort | hiv-1 gp120 n-linked glycosylation differs between plasma and leukocyte compartments |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2265691/ https://www.ncbi.nlm.nih.gov/pubmed/18215327 http://dx.doi.org/10.1186/1743-422X-5-14 |
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