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PMID: 19962198 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Heat shock proteins on the human sperm surface.

Journal of reproductive immunology ·Vol. 84 ·No. 1 ·2010-01-00 ·Pages 32-40

Naaby-Hansen S, Herr JC

Abstract

The sperm plasma membrane is known to be critical to fertilization and to be highly regionalized into domains of head, mid- and principal pieces. However, the molecular composition of the sperm plasma membrane and its alterations during genital tract passage, capacitation and the acrosome reaction remains to be fully dissected. A two-dimensional gel-based proteomic study previously identified 98 human sperm proteins which were accessible for surface labelling with both biotin and radioiodine. In this report twelve dually labelled protein spots were excised from stained gels or PDVF membranes and analysed by mass spectrometry (MS) and Edman degradation. Seven members from four different heat shock protein (HSP) families were identified including HYOU1 (ORP150), HSPC1 (HSP86), HSPA5 (Bip), HSPD1 (HSP60), and several isoforms of the two testis-specific HSP70 chaperones HSPA2 and HSPA1L. An antiserum raised against the testis-specific HSPA2 chaperone reacted with three 65kDa HSPA2 isoforms and three high molecular weight surface proteins (78-79kDa, 84kDa and 90-93kDa). These proteins, together with seven 65kDa HSP70 forms, reacted with human anti-sperm IgG antibodies that blocked in vitro fertilization in humans. Three of these surface biotinylated human sperm antigens were immunoprecipitated with a rabbit antiserum raised against a linear peptide epitope in Chlamydia trachomatis HSP70. The results indicate diverse HSP chaperones are accessible for surface labelling on human sperm. Some of these share epitopes with C. trachomatis HSP70, suggesting an association between genital tract infection, immunity to HSP70 and reproductive failure.

MeSH Terms
Acrosome Reaction/immunology Animals Antigens/immunology Cell Membrane/metabolism Chlamydia Infections/immunology Endoplasmic Reticulum Chaperone BiP Epitopes/immunology Female Heat-Shock Proteins/chemistry,metabolism Humans Male Molecular Chaperones/chemistry,metabolism Rabbits Spermatozoa/chemistry,metabolism
Chemicals
Antigens Endoplasmic Reticulum Chaperone BiP Epitopes HSPA5 protein, human Heat-Shock Proteins Molecular Chaperones
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Naaby-Hansen Soren
Department of Clinical Immunology, Aalborg Sygehus, Aarhus University Hospital, Denmark. [email protected]
Herr John C
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Article Info
Journal
Journal of reproductive immunology
Abbr.
J Reprod Immunol
ISSN
1872-7603
Published
2010-01-00
Epub
2009-00-03
Pages
32-40
Language
English
Region
Ireland
NLM ID
8001906
PMCID
PMC2898571
Subset
IM
Grants
NCRR NIH HHS · P51 RR000166 · United States
NICHD NIH HHS · U54 HD029099-09 · United States
NICHD NIH HHS · U54 HD029099-070003 · United States
NICHD NIH HHS · U54 HD029099-08 · United States
NICHD NIH HHS · U54 HD029099-060003 · United States
NICHD NIH HHS · U54 HD29099 · United States
FIC NIH HHS · D43 TW000654-05 · United States
FIC NIH HHS · D43 TW000654 · United States
NICHD NIH HHS · U54 HD029099 · United States
NICHD NIH HHS · U54 HD029099-080003 · United States
NCRR NIH HHS · P51 RR000166-38S10110 · United States
NCRR NIH HHS · P51 RR000166-400110 · United States
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