title: Cyclophilins and nucleoporins are required for infection mediated by capsids from circulating HIV-2 primary isolates.
abstract: HIV-2 groups have emerged from sooty mangabey SIV and entered the human population in Africa on several separate occasions. Compared to world pandemic HIV-1 that arose from the chimpanzee SIVcpz virus, the SIVsm-derived HIV-2, largely confined to West Africa, is less replicative, less transmissible and less pathogenic. Here, we evaluated the interactions between host cellular factors, which control HIV-1 infection and target the capsid, and HIV-2 capsids obtained from primary isolates from patients with different disease progression status. We showed that, like HIV-1, all HIV-2 CA we tested exhibited a dependence on cyclophilin A. However, we observed no correlation between HIV-2 viremia and susceptibility to hu-TRIM5alpha or dependence to CypA. Finally, we found that all CA from HIV-2 primary isolates exploit Nup358 and Nup153 for nucleus transposition. Altogether, these findings indicate that the ability to use the two latter nucleoporins is essential to infection of human cells for both HIV-1 and HIV-2. This dependence provides another molecular target that could be used for antiviral strategies against both HIV-1 and 2, based on both nucleoporins.
authors.affiliation: Institut de Génétique Moléculaire de Montpellier, UMR 5535 CNRS, 1919 route de Mende, 34293 Montpellier cedex 5, France; Université de Montpellier, 163 rue Auguste Broussonnet, 34090 Montpellier, France.
authors.forename: João I
authors.initials: JI
authors.lastname: Mamede
authors.affiliation: Laboratoire de Virologie, AP-HP Groupe Hospitalier Bichat-Claude Bernard, HUPNVS, Université Paris Diderot, Sorbonne Paris Cité, EA4409, 75018, Paris, France.
authors.forename: Florence
authors.initials: F
authors.lastname: Damond
authors.affiliation: Institut de Génétique Moléculaire de Montpellier, UMR 5535 CNRS, 1919 route de Mende, 34293 Montpellier cedex 5, France; Université de Montpellier, 163 rue Auguste Broussonnet, 34090 Montpellier, France.
authors.forename: Ariel de
authors.initials: A
authors.lastname: Bernardo
authors.affiliation: Laboratoire de Virologie, AP-HP Groupe Hospitalier Bichat-Claude Bernard, HUPNVS, Université Paris Diderot, Sorbonne Paris Cité, EA4409, 75018, Paris, France.
authors.forename: Sophie
authors.initials: S
authors.lastname: Matheron
authors.affiliation: Laboratoire de Virologie, AP-HP Groupe Hospitalier Bichat-Claude Bernard, HUPNVS, Université Paris Diderot, Sorbonne Paris Cité, EA4409, 75018, Paris, France.
authors.forename: Diane
authors.initials: D
authors.lastname: Descamps
authors.affiliation: Institut de Génétique Moléculaire de Montpellier, UMR 5535 CNRS, 1919 route de Mende, 34293 Montpellier cedex 5, France; Université de Montpellier, 163 rue Auguste Broussonnet, 34090 Montpellier, France.
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Battini
authors.affiliation: Institut de Génétique Moléculaire de Montpellier, UMR 5535 CNRS, 1919 route de Mende, 34293 Montpellier cedex 5, France; Université de Montpellier, 163 rue Auguste Broussonnet, 34090 Montpellier, France.
authors.forename: Marc
authors.initials: M
authors.lastname: Sitbon
authors.affiliation: Institut de Génétique Moléculaire de Montpellier, UMR 5535 CNRS, 1919 route de Mende, 34293 Montpellier cedex 5, France; Université de Montpellier, 163 rue Auguste Broussonnet, 34090 Montpellier, France.
authors.forename: Valérie
authors.initials: V
authors.lastname: Courgnaud
mesh_terms: D000354:Africa, Western; D000818:Animals; D000090103:Antiviral Restriction Factors; D002213:Capsid / Q000378:metabolism / Q000502:physiology; D002352:Carrier Proteins / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism / Q000821:virology; D021984:Cyclophilin A / Q000378:metabolism*; D057809:HEK293 Cells; D015658:HIV Infections / Q000378:metabolism / Q000821:virology*; D015497:HIV-1 / Q000378:metabolism / Q000472:pathogenicity; D015498:HIV-2 / Q000378:metabolism / Q000472:pathogenicity*; D006801:Humans; D051379:Mice; D018832:Molecular Chaperones / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000378:metabolism*; D000070584:Tripartite Motif Proteins; D044767:Ubiquitin-Protein Ligases; D014779:Virus Replication
chemical_list: D000090103:Antiviral Restriction Factors; D002352:Carrier Proteins; D018832:Molecular Chaperones; C079377:NUP153 protein, human; D028861:Nuclear Pore Complex Proteins; D000070584:Tripartite Motif Proteins; C094493:ran-binding protein 2; C477346:TRIM5 protein, human; D044767:Ubiquitin-Protein Ligases; D021984:Cyclophilin A