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Biology of Reproduction 61, 1184-1197 (1999)
© 1999 Society for the Study of Reproduction, Inc.

Articles

FSP95, A Testis-Specific 95-Kilodalton Fibrous Sheath Antigen That Undergoes Tyrosine Phosphorylation in Capacitated Human Spermatozoa1

Arabinda Mandala, Søren Naaby-Hansena, Michael J. Wolkowicza, Ken Klotza, Jagathpala Shettya, Jacques D. Retiefb, Scott A. Coonroda, Michael Kinterc, Nicholas Shermanc, Fred Cesara, Charles J. Flickingera, and John C. Herr2,a

a Center for Recombinant Gamete Contraceptive Vaccinogens, Department of Cell Biology, University of Virginia, Charlottesville, Virginia 22908 b Academic Computing Health Sciences, University of Virginia, Charlottesville, Virginia 22908 c W.M. Keck Biomedical Mass Spectrometry Laboratory, School of Medicine, University of Virginia, Charlottesville, Virginia 22908

Protein tyrosine phosphorylation has been associated with both capacitation and motility of mammalian sperm. During capacitation, human spermatozoa undergo tyrosine phosphorylation of a characteristic set of proteins, only one of which has thus far been cloned and localized. We report here the sequence of a fibrous sheath protein of 95 kDa (FSP95) that undergoes tyrosine phosphorylation during capacitation of human spermatozoa and has similarity to sperm A-kinase anchor proteins (AKAPs). FSP95 is both auto- and iso-antigenic in humans as it is recognized by sera containing antisperm antibodies from infertile men and women. The 853-residue protein has a calculated molecular weight of 94.6 kDa and an isoelectric point (pI) of 6.0, and it contains multiple potential phosphorylation sites for protein kinase C and casein kinase II as well as one potential tyrosine kinase phosphorylation site at amino acid 435. The sequence has amino acid homology to mouse sperm fibrous sheath AKAP82 (pro-mAKAP82, 34% identity) and to human sperm fibrous sheath AKAP82 (pro-hAKAP82, 32% identity). The gene encoding FSP95 has 5 exons separated by 4 introns and is located on chromosome 12 at locus p13.3. Northern analysis detected a single transcript of ~3.0 kilobases, and Northern dot blot analysis of 50 human tissues revealed FSP95 mRNA expression only in testis. By employing sperm immobilization, indirect immunofluorescence, and immunoelectron microscopy with antisera to purified recombinant FSP95, the protein was localized to the ribs of the fibrous sheath in the principal piece of the sperm tail. FSP95 is the second fibrous sheath protein to be cloned, sequenced and localized in human spermatozoa.

1 This work was supported in part by grants from Fogarty International Center D43 TW/HD 00654, NIH HD U54 29099, P30 28934, the Andrew W. Mellon Foundation, and Schering AG.

2 Correspondence: John C. Herr, Department of Cell Biology, University of Virginia Health Sciences Center, Box 439, Charlottesville, VA 22908. FAX: 804 982 3912; jch7k{at}virginia.edu




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