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Members of the 70 kDa heat shock protein family specifically recognize sulfoglycolipids: Role in gamete recognition and mycoplasma‐related infertility
Author(s) -
Boulanger J.,
Faulds D.,
Eddy E. M.,
Lingwood C. A.
Publication year - 1995
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041650103
Subject(s) - biology , gamete , bacterial adhesin , heat shock protein , male infertility , glycolipid , infertility , sperm , in vitro , hsp70 , immunology , microbiology and biotechnology , genetics , gene , escherichia coli , pregnancy
We have previously shown that several mycoplasma species associated with infertility bind specifically to sulfated glycolipids isolated from the mammalian reproductive tract. We now show that a germ cell‐specific sulfoglycolipid binding protein (SLIP 1), which is a potent inhibitor of sperm/egg binding in vitro, is immunologically related to the heat shock protein (Hsp) 70 family of stress proteins and that Hsps are surface antigens in male germ cells. Our present data demonstrate that several mycoplasma and mammalian Hsps share this glycolipid binding specificity in vitro, and suggest that surface Hsps can function as adhesins which mediate sulfoglycolipid recognition in infectious disease and normal reproductive physiology. © 1995 Wiley‐Liss Inc.