title: HIV-1 Vpu affects the anterograde transport and the glycosylation pattern of NTB-A.
abstract: HIV-1 Vpu induces downregulation of cell surface NTB-A to evade lysis of HIV-1 infected cells by NK cells. Here we show that Vpu affects the anterograde transport and the glycosylation pattern of NTB-A by a mechanism that is distinct from the Vpu induced downregulation of CD4 and tetherin. In the presence of Vpu, only the high mannose form of NTB-A was detectable, suggesting that Vpu prevented the formation of the mature form of NTB-A. This phenomenon is associated with the ability of Vpu to downregulate cell surface NTB-A by retention of NTB-A within the Golgi-compartment. Furthermore, the Vpu-mediated effect on NTB-A glycosylation is highly conserved among Vpu proteins derived from HIV-1 and SIV and corresponds to the level of downregulation of NTB-A. Together, these results suggest that the reduction of NTB-A from the cell surface is associated with the Vpu-mediated effect on the glycosylation pattern of newly synthesized NTB-A molecules.
authors.affiliation: Institute of Virology, University of Erlangen-Nuremberg, Germany.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Bolduan
authors.forename: Philipp
authors.initials: P
authors.lastname: Hubel
authors.forename: Tatjana
authors.initials: T
authors.lastname: Reif
authors.forename: Veronika
authors.initials: V
authors.lastname: Lodermeyer
authors.forename: Kristin
authors.initials: K
authors.lastname: Höhne
authors.forename: Joëlle V
authors.initials: JV
authors.lastname: Fritz
authors.forename: Daniel
authors.initials: D
authors.lastname: Sauter
authors.forename: Frank
authors.initials: F
authors.lastname: Kirchhoff
authors.forename: Oliver T
authors.initials: OT
authors.lastname: Fackler
authors.forename: Michael
authors.initials: M
authors.lastname: Schindler
authors.forename: Ulrich
authors.initials: U
authors.lastname: Schubert
mesh_terms: D015703:Antigens, CD / Q000378:metabolism*; D002460:Cell Line; D015536:Down-Regulation; D015870:Gene Expression; D006031:Glycosylation; D015497:HIV-1 / Q000472:pathogenicity*; D054884:Host-Pathogen Interactions; D054298:Human Immunodeficiency Virus Proteins / Q000378:metabolism*; D006801:Humans; D057131:Immune Evasion; D021381:Protein Transport; D011956:Receptors, Cell Surface / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D000071176:Signaling Lymphocytic Activation Molecule Family; D000071177:Signaling Lymphocytic Activation Molecule Family Member 1; D054334:Viral Regulatory and Accessory Proteins / Q000378:metabolism*; D000086082:Viroporin Proteins
chemical_list: D015703:Antigens, CD; D054298:Human Immunodeficiency Virus Proteins; D011956:Receptors, Cell Surface; D000071176:Signaling Lymphocytic Activation Molecule Family; D000071177:Signaling Lymphocytic Activation Molecule Family Member 1; D054334:Viral Regulatory and Accessory Proteins; C000604060:SLAMF6 protein, human; C514859:vpu protein, Human immunodeficiency virus 1; D000086082:Viroporin Proteins