A 60 kD heat-shock protein-like molecule interacts with the HIV transmembrane glycoprotein gp41
| Autor: | Xiaojie Zhu, Barbara Jöbstl, George Füst, Cornelia Speth, Gabriele Stöckl, Mechthild Mair, Zoltán Prohászka, Manfred P. Dierich |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Vesicle-associated membrane protein 8
animal structures L1 T-Lymphocytes Immunology chemical and pharmacologic phenomena Plasma protein binding Gp41 complex mixtures Monocytes Cell membrane Protein A/G medicine Humans Molecular Biology Cells Cultured Glycoproteins B-Lymphocytes biology Binding protein fungi virus diseases Chaperonin 60 Molecular biology HIV Envelope Protein gp41 Transmembrane protein medicine.anatomical_structure Biochemistry HIV-1 biology.protein Protein Binding |
| Zdroj: | Molecular Immunology. 36:619-628 |
| ISSN: | 0161-5890 |
| DOI: | 10.1016/s0161-5890(99)00082-6 |
| Popis: | The heat-shock protein hsp60 is typically found in mitochondria, but, in smaller amounts, also in the cell cytoplasm and associated with the cell membrane. Since heat-shock proteins are known to interact with a variety of molecules and since purified HIV-1 particles were described to contain hsp60 molecules, we tested the possibility that a previously described putative receptor for HIV transmembrane protein gp41 is identical to hsp60. The gp41-binding human protein P62 was purified from H9 and Raji cell lysates by a gp41-coupled affinity column. We could show crossreactivity of both polyclonal and monoclonal anti-hsp60 antibodies with the purified P62. In addition we analyzed binding of P18, a soluble gp41 fragment harboring the extracellular domain (Env aa539-684), to recombinant hsp60. Hsp60 bound well to P18-coated ELISA plates whereas HIV-1 surface protein gp120 induced no binding of hsp60. Preincubation of hsp60 with gp41 abolished the binding. The possible role of this molecule as a cofactor in the pathogenesis of HIV disease is discussed. |
| Databáze: | OpenAIRE |
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