A 60 kD heat-shock protein-like molecule interacts with the HIV transmembrane glycoprotein gp41

Speth, Cornelia and Prohászka, Zoltán and Mair, Mechthild and Stöckl, Gabriele and Zhu, Xiaojie and Jöbstl, Barbara and Füst, George and Dierich, Manfred P. (1999) A 60 kD heat-shock protein-like molecule interacts with the HIV transmembrane glycoprotein gp41. MOLECULAR IMMUNOLOGY, 36 (9). pp. 619-628. ISSN 0161-5890

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Abstract

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.

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