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HIV-1 Tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region

AIDS · 1997 · Vol. 11(12) · pp. 1421–1431

Hsiao C. Chang✉(National Institutes of Health)Felipe Samaniego(National Institutes of Health)Bala C. Nair(Advanced Bioscience Laboratories (United States))Luigi Buonaguro(Istituto Nazionale Tumori IRCCS "Fondazione G. Pascale")Barbara Ensoli(Istituto Superiore di Sanità)

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Abstract

These results demonstrate that Tat exits from intact cells through a leaderless secretion pathway which shares several features with that of acid FGF or bFGF. The released Tat binds to HSPG through its basic region and this determines its storage into the ECM, as occurs for bFGF.

HIV Research and Treatment Glycosylation and Glycoproteins Research Monoclonal and Polyclonal Antibodies ResearchBrefeldin AFurinHeparan sulfateExtracellular matrixHeparinExtracellularBiochemistryChemistryCell biologyMolecular biology

MeSH terms

AnimalsBinding SitesCell SurvivalExtracellular MatrixInterleukin-1Recombinant ProteinsHIV-1Gene Products, tatFibroblast Growth Factor 1Fibroblast Growth Factor 2ApoptosisCOS CellsHeparan Sulfate Proteoglycanstat Gene Products, Human Immunodeficiency Virus

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The mystery of nonclassical protein secretion