Important note: Information in this article was accurate in 1994. The state of the art may have changed since the publication date.
Are there roles for heat shock proteins in the replication of HIV and SIV?
Symp Nonhum Primate Models AIDS. 1993 Sep 19-22;11:abstract no. 34. Unique Identifier : AIDSLINE PRIM11/94191628 Bartz SR; Pauza CD; Ivanyi J; Jindal S; Welch WJ; Malkovsky M; Dept. of Medical Microbiology and Immunology, Univ. of Wisconsin.
Abstract:
The role of host cell proteins in the assembly of, the pathogenesis of, and the immune response to HIV and SIV is not well understood. Heat shock proteins (Hsp's) are potentially important for viral production because of their known functions in cellular protein maturation and assembly of macromolecular complexes. Also, Hsp's are strongly immunogenic for both T and B cell responses. We have previously reported that the level of Hsp's are increased in cells infected with either HIV or SIV. Here we investigated the possible physical association of Hsp's with HIV and SIV. Western blotting revealed an Hsp60 related protein associated with purified HIV and SIV. Other Hsp's such as Hsp70 and Hsp28 were not detected. The Hsp60 related protein reacts with the monoclonal antibody (mAb) ML30, specific for mycobacterial Hsp65 and human Hsp58, but not with other mAb that are specific for the mitochondrial form of Hsp58. Interestingly, the virion associated protein is approximately 75 kD, which differs from the reported molecular weights of members of the Hsp60 family. A sequence search revealed that the specific epitope recognized by ML30 is not present in any of the three reading frames of HIV-1. This indicates that the 75 kD protein is of cellular origin. In addition to ML30, a polyclonal rabbit serum generated to the cytoplasmic form of Hsp58 (but not mitochondrial Hsp58-specific antiserum) recognizes what appears to be the 75 kD virus associated protein. Western blot analysis of two-dimensional gels of purified virion preparations revealed that the Hsp60 related protein has the same isoelectric focusing pattern in both HIV and SIV, supporting the cellular origin of this protein. Phase separation of virion preps with Triton X-114 showed that this ML30 reactive protein is associated with the core proteins of the virus, which suggests that it may be involved in the assembly of virions.
Keywords: Antibodies, Monoclonal Antibody Specificity B-Lymphocytes/IMMUNOLOGY Blotting, Western Electrophoresis, Gel, Two-Dimensional Heat-Shock Proteins/ANALYSIS/BIOSYNTHESIS/*METABOLISM Human HIV/ISOLATION & PURIF/*PHYSIOLOGY HIV-1/GENETICS Isoelectric Focusing Mycobacterium/METABOLISM SIV/ISOLATION & PURIF/*PHYSIOLOGY T-Lymphocytes/IMMUNOLOGY *Virus Replication ABSTRACT 940730
M9470890
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