Lineage-specific differences between the gp120 inner domain layer 3 of human immunodeficiency virus and that of simian immunodeficiency virus

Shilei Ding, Halima Medjahed, Jérémie Prévost, Mathieu Coutu, Shi-Hua Xiang, Andrés Finzi

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Binding of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV) gp120 exterior envelope glycoprotein to CD4 triggers conformational changes in gp120 that promote its interaction with one of the chemokine receptors, usually CCR5, ultimately leading to gp41-mediated virus-cell membrane fusion and entry. We previously described that topological layers (layer 1, layer 2, and layer 3) in the gp120 inner domain contribute to gp120-trimer association in the unliganded state but also help secure CD4 binding. Relative to layer 1 of HIV-1 gp120, the SIVmac239 gp120 layer 1 plays a more prominent role in maintaining gp120-trimer association but is minimally involved in promoting CD4 binding, which could be explained by the existence of a well-conserved tryptophan at position 375 (Trp 375) in HIV-2/SIVsmm. In this study, we investigated the role of SIV layer 3 in viral entry, cell-to-cell fusion, and CD4 binding. We observed that a network of interactions involving some residues of the β8-α5 region in SIVmac239 layer 3 may contribute to CD4 binding by helping shape the nearby Phe 43 cavity, which directly contacts CD4. In summary, our results suggest that layer 3 in SIV has a greater impact on CD4 binding than in HIV-1. This work defines lineage-specific differences in layer 3 from HIV-1 and that from SIV.

Original languageEnglish (US)
Pages (from-to)10065-10073
Number of pages9
JournalJournal of virology
Volume90
Issue number22
DOIs
StatePublished - Jan 1 2016

Fingerprint

Simian immunodeficiency virus
Simian Immunodeficiency Virus
Human immunodeficiency virus
Human immunodeficiency virus 1
HIV-1
HIV
Cell Fusion
Human immunodeficiency virus 2
Virus Internalization
cell fusion
HIV-2
Chemokine Receptors
Tryptophan
tryptophan
cell membranes
glycoproteins
Glycoproteins
Cell Membrane
viruses
cells

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Cite this

Lineage-specific differences between the gp120 inner domain layer 3 of human immunodeficiency virus and that of simian immunodeficiency virus. / Ding, Shilei; Medjahed, Halima; Prévost, Jérémie; Coutu, Mathieu; Xiang, Shi-Hua; Finzi, Andrés.

In: Journal of virology, Vol. 90, No. 22, 01.01.2016, p. 10065-10073.

Research output: Contribution to journalArticle

Ding, Shilei ; Medjahed, Halima ; Prévost, Jérémie ; Coutu, Mathieu ; Xiang, Shi-Hua ; Finzi, Andrés. / Lineage-specific differences between the gp120 inner domain layer 3 of human immunodeficiency virus and that of simian immunodeficiency virus. In: Journal of virology. 2016 ; Vol. 90, No. 22. pp. 10065-10073.
@article{4d3887ff1d124785b02e87fe7a181052,
title = "Lineage-specific differences between the gp120 inner domain layer 3 of human immunodeficiency virus and that of simian immunodeficiency virus",
abstract = "Binding of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV) gp120 exterior envelope glycoprotein to CD4 triggers conformational changes in gp120 that promote its interaction with one of the chemokine receptors, usually CCR5, ultimately leading to gp41-mediated virus-cell membrane fusion and entry. We previously described that topological layers (layer 1, layer 2, and layer 3) in the gp120 inner domain contribute to gp120-trimer association in the unliganded state but also help secure CD4 binding. Relative to layer 1 of HIV-1 gp120, the SIVmac239 gp120 layer 1 plays a more prominent role in maintaining gp120-trimer association but is minimally involved in promoting CD4 binding, which could be explained by the existence of a well-conserved tryptophan at position 375 (Trp 375) in HIV-2/SIVsmm. In this study, we investigated the role of SIV layer 3 in viral entry, cell-to-cell fusion, and CD4 binding. We observed that a network of interactions involving some residues of the β8-α5 region in SIVmac239 layer 3 may contribute to CD4 binding by helping shape the nearby Phe 43 cavity, which directly contacts CD4. In summary, our results suggest that layer 3 in SIV has a greater impact on CD4 binding than in HIV-1. This work defines lineage-specific differences in layer 3 from HIV-1 and that from SIV.",
author = "Shilei Ding and Halima Medjahed and J{\'e}r{\'e}mie Pr{\'e}vost and Mathieu Coutu and Shi-Hua Xiang and Andr{\'e}s Finzi",
year = "2016",
month = "1",
day = "1",
doi = "10.1128/JVI.01215-16",
language = "English (US)",
volume = "90",
pages = "10065--10073",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "22",

}

TY - JOUR

T1 - Lineage-specific differences between the gp120 inner domain layer 3 of human immunodeficiency virus and that of simian immunodeficiency virus

AU - Ding, Shilei

AU - Medjahed, Halima

AU - Prévost, Jérémie

AU - Coutu, Mathieu

AU - Xiang, Shi-Hua

AU - Finzi, Andrés

PY - 2016/1/1

Y1 - 2016/1/1

N2 - Binding of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV) gp120 exterior envelope glycoprotein to CD4 triggers conformational changes in gp120 that promote its interaction with one of the chemokine receptors, usually CCR5, ultimately leading to gp41-mediated virus-cell membrane fusion and entry. We previously described that topological layers (layer 1, layer 2, and layer 3) in the gp120 inner domain contribute to gp120-trimer association in the unliganded state but also help secure CD4 binding. Relative to layer 1 of HIV-1 gp120, the SIVmac239 gp120 layer 1 plays a more prominent role in maintaining gp120-trimer association but is minimally involved in promoting CD4 binding, which could be explained by the existence of a well-conserved tryptophan at position 375 (Trp 375) in HIV-2/SIVsmm. In this study, we investigated the role of SIV layer 3 in viral entry, cell-to-cell fusion, and CD4 binding. We observed that a network of interactions involving some residues of the β8-α5 region in SIVmac239 layer 3 may contribute to CD4 binding by helping shape the nearby Phe 43 cavity, which directly contacts CD4. In summary, our results suggest that layer 3 in SIV has a greater impact on CD4 binding than in HIV-1. This work defines lineage-specific differences in layer 3 from HIV-1 and that from SIV.

AB - Binding of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV) gp120 exterior envelope glycoprotein to CD4 triggers conformational changes in gp120 that promote its interaction with one of the chemokine receptors, usually CCR5, ultimately leading to gp41-mediated virus-cell membrane fusion and entry. We previously described that topological layers (layer 1, layer 2, and layer 3) in the gp120 inner domain contribute to gp120-trimer association in the unliganded state but also help secure CD4 binding. Relative to layer 1 of HIV-1 gp120, the SIVmac239 gp120 layer 1 plays a more prominent role in maintaining gp120-trimer association but is minimally involved in promoting CD4 binding, which could be explained by the existence of a well-conserved tryptophan at position 375 (Trp 375) in HIV-2/SIVsmm. In this study, we investigated the role of SIV layer 3 in viral entry, cell-to-cell fusion, and CD4 binding. We observed that a network of interactions involving some residues of the β8-α5 region in SIVmac239 layer 3 may contribute to CD4 binding by helping shape the nearby Phe 43 cavity, which directly contacts CD4. In summary, our results suggest that layer 3 in SIV has a greater impact on CD4 binding than in HIV-1. This work defines lineage-specific differences in layer 3 from HIV-1 and that from SIV.

UR - http://www.scopus.com/inward/record.url?scp=84995469397&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84995469397&partnerID=8YFLogxK

U2 - 10.1128/JVI.01215-16

DO - 10.1128/JVI.01215-16

M3 - Article

C2 - 27535053

AN - SCOPUS:84995469397

VL - 90

SP - 10065

EP - 10073

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 22

ER -