DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4.
Mannose-binding C-type lectin receptors, expressed on Langerhans cells and subepithelial dendritic cells (DCs) of cervico-vaginal tissues, play an important role in HIV-1 capture and subsequent dissemination to lymph nodes. DC-SIGN has been implicated in both productive infection of DCs and the DC-m...
Saved in:
| Main Authors: | , , , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2011-01-01
|
| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0028307&type=printable |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849470646928539648 |
|---|---|
| author | Karolin Hijazi Yufei Wang Carlo Scala Simon Jeffs Colin Longstaff Daniel Stieh Beth Haggarty Guido Vanham Dominique Schols Jan Balzarini Ian M Jones James Hoxie Robin Shattock Charles G Kelly |
| author_facet | Karolin Hijazi Yufei Wang Carlo Scala Simon Jeffs Colin Longstaff Daniel Stieh Beth Haggarty Guido Vanham Dominique Schols Jan Balzarini Ian M Jones James Hoxie Robin Shattock Charles G Kelly |
| author_sort | Karolin Hijazi |
| collection | DOAJ |
| description | Mannose-binding C-type lectin receptors, expressed on Langerhans cells and subepithelial dendritic cells (DCs) of cervico-vaginal tissues, play an important role in HIV-1 capture and subsequent dissemination to lymph nodes. DC-SIGN has been implicated in both productive infection of DCs and the DC-mediated trans infection of CD4(+) T cells that occurs in the absence of replication. However, the molecular events that underlie this efficient transmission have not been fully defined. In this study, we have examined the effect of the extracellular domains of DC-SIGN and Langerin on the stability of the interaction of the HIV-1 envelope glycoprotein with CD4 and also on replication in permissive cells. Surface plasmon resonance analysis showed that DC-SIGN increases the binding affinity of trimeric gp140 envelope glycoproteins to CD4. In contrast, Langerin had no effect on the stability of the gp140:CD4 complex. In vitro infection experiments to compare DC-SIGN enhancement of CD4-dependent and CD4-independent strains demonstrated significantly lower enhancement of the CD4-independent strain. In addition DC-SIGN increased the relative rate of infection of the CD4-dependent strain but had no effect on the CD4-independent strain. DC-SIGN binding to the HIV envelope protein effectively increases exposure of the CD4 binding site, which in turn contributes to enhancement of infection. |
| format | Article |
| id | doaj-art-6ffdc28f18324ddeb324bcee8e41573b |
| institution | Kabale University |
| issn | 1932-6203 |
| language | English |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-6ffdc28f18324ddeb324bcee8e41573b2025-08-20T03:25:07ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01612e2830710.1371/journal.pone.0028307DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4.Karolin HijaziYufei WangCarlo ScalaSimon JeffsColin LongstaffDaniel StiehBeth HaggartyGuido VanhamDominique ScholsJan BalzariniIan M JonesJames HoxieRobin ShattockCharles G KellyMannose-binding C-type lectin receptors, expressed on Langerhans cells and subepithelial dendritic cells (DCs) of cervico-vaginal tissues, play an important role in HIV-1 capture and subsequent dissemination to lymph nodes. DC-SIGN has been implicated in both productive infection of DCs and the DC-mediated trans infection of CD4(+) T cells that occurs in the absence of replication. However, the molecular events that underlie this efficient transmission have not been fully defined. In this study, we have examined the effect of the extracellular domains of DC-SIGN and Langerin on the stability of the interaction of the HIV-1 envelope glycoprotein with CD4 and also on replication in permissive cells. Surface plasmon resonance analysis showed that DC-SIGN increases the binding affinity of trimeric gp140 envelope glycoproteins to CD4. In contrast, Langerin had no effect on the stability of the gp140:CD4 complex. In vitro infection experiments to compare DC-SIGN enhancement of CD4-dependent and CD4-independent strains demonstrated significantly lower enhancement of the CD4-independent strain. In addition DC-SIGN increased the relative rate of infection of the CD4-dependent strain but had no effect on the CD4-independent strain. DC-SIGN binding to the HIV envelope protein effectively increases exposure of the CD4 binding site, which in turn contributes to enhancement of infection.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0028307&type=printable |
| spellingShingle | Karolin Hijazi Yufei Wang Carlo Scala Simon Jeffs Colin Longstaff Daniel Stieh Beth Haggarty Guido Vanham Dominique Schols Jan Balzarini Ian M Jones James Hoxie Robin Shattock Charles G Kelly DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4. PLoS ONE |
| title | DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4. |
| title_full | DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4. |
| title_fullStr | DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4. |
| title_full_unstemmed | DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4. |
| title_short | DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4. |
| title_sort | dc sign increases the affinity of hiv 1 envelope glycoprotein interaction with cd4 |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0028307&type=printable |
| work_keys_str_mv | AT karolinhijazi dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT yufeiwang dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT carloscala dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT simonjeffs dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT colinlongstaff dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT danielstieh dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT bethhaggarty dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT guidovanham dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT dominiqueschols dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT janbalzarini dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT ianmjones dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT jameshoxie dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT robinshattock dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 AT charlesgkelly dcsignincreasestheaffinityofhiv1envelopeglycoproteininteractionwithcd4 |