MEMBERS OF THE 70 KDA HEAT-SHOCK PROTEIN FAMILY SPECIFICALLY RECOGNIZE SULFOGLYCOLIPIDS - ROLE IN GAMETE RECOGNITION AND MYCOPLASMA-RELATEDINFERTILITY

We have previously shown that several mycoplasma species associated wi th infertility bind specifically to sulfated glycolipids isolated from the mammalian reproductive tract. We now show that a germ cell-specif ic sulfoglycolipid binding protein (SLIP 1), which is a potent inhibit or of sperm/egg binding in vitro, is immunologically related to the he at shock protein(Hsp) 70 family of stress proteins and that Hsps are s urface antigens in male germ cells. Our present data demonstrate that several mycoplasma and mammalian Hsps share this glycolipid binding sp ecificity in vitro, and suggest that surface Hsps can function as adhe sins which mediate sulfoglycolipid recognition in infectious disease a nd normal reproductive physiology. (C) 1995 Wiley-Liss, Inc.