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Gene Review

ACRV1  -  acrosomal vesicle protein 1

Homo sapiens

Synonyms: Acrosomal protein SP-10, Acrosomal vesicle protein 1, D11S4365, SP-10, SPACA2
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Disease relevance of ACRV1

  • A recombinant SP-10 fusion protein was produced in an Escherichia coli expression vector and used to generate a polyclonal antiserum [1].
  • These data demonstrate that the carrier-free T1-SP10 synthetic peptide construct can induce high titers of neutralizing anti-HIV antibody responses and PBMC proliferative responses to HIV in primates [2].
  • When combined in a trivalent inoculum, T1-SP10 peptides from HIV-1 isolates IIIB, MN, and RF evoked a high titered neutralizing antibody response to isolates IIIB, MN, and RF in goats and as well induced immune T cells to undergo blast transformation in the presence of peptides derived from gp120 of all three HIV isolates [3].
  • A monoclonal antibody to human SP-10 inhibits in vitro the binding of human sperm to hamster oolemma but not to human Zona pellucida [4].
  • Furthermore, we demonstrated that the oolemmal ligands of human SP-10 did not include beta(1) integrins, the most promising candidates for oocyte ligands involved in sperm-oolemma binding, based on the findings of a human sperm-cultured cell binding assay using F9 mouse embryonal carcinoma cells and F9-transformed cells lacking beta(1) integrins [4].

High impact information on ACRV1

  • Antibodies to both portions of suREJ3 localize exclusively to the plasma membrane over the acrosomal vesicle [5].
  • Sea urchin sperm contain a single exocytotic vesicle, the acrosomal vesicle, whose contents are exposed during the acrosome reaction [6].
  • We have previously described a synthetic peptide (T1-SP10) derived from two noncontiguous regions of HTLVIIIB envelope gp120 (T1, amino acids 428-443; SP10, amino acids 303-321) that induced type-specific anti-HIV neutralizing antibodies and T cell proliferative responses against native HIV gp120 when used as a carrier-free immunogen in goats [2].
  • Sera from all four animals given T1-SP10 in IFA or threonyl-MDP neutralized infection by HTLVIIIB and blocked virus-dependent cell fusion events [2].
  • In previous studies, we have used antisera raised to envelope (env)-gene-encoded synthetic peptides to identify a region of (HIV) glycoprotein (gp) 120 env protein designated SP10 that contains a type-specific neutralizing determinant [3].

Chemical compound and disease context of ACRV1

  • The benzamide derivative N-[1-(7-tert-Butyl-1H-indol-3-ylmethyl)-2-(4-cyclopropanecarbonyl-3-methyl-piperazin-1-yl)-2-oxo-ethyl]-4-nitro-benzamide (SP-10) reduces HIV-1 infectivity in vitro by modifying actin dynamics [7].
  • Fipronil provided delayed toxicity at 21-23 degrees C with SP10 values ranging from 270 to 960 min [8].

Biological context of ACRV1

  • Refinement of the localization of the gene for human intraacrosomal protein SP-10 (ACRV1) to the junction of bands q23-->q24 of chromosome 11 by nonisotopic in situ hybridization [9].
  • cDNAs coding for the intra-acrosomal protein SP-10 were cloned and characterized as a first step in understanding the expression of this antigen during spermatogenesis [1].
  • Interestingly, cDNA SP-10-10 has an internal 57-base pair (19 amino acids) in-frame deletion that is not present in SP-10-5, suggesting that alternative splicing generates more than one SP-10 mRNA [1].
  • Recombinant SP-10 is currently being tested as a contraceptive vaccine immunogen on the basis of its tissue specificity as well as functional assays indicating that anti-SP-10 antisera inhibit sperm-egg interactions [10].
  • Mapping and sequencing of the 8-kb SP-10 gene show that the SP-10 mRNA consists of exons of 119, 487, 113, and 390 bp with each exon coding for a distinct structural domain within the SP-10 protein [10].

Anatomical context of ACRV1


Associations of ACRV1 with chemical compounds

  • After induction of the acrosome reaction with the ionophore A23187, SP-10 remained displayed on the sperm head in association with the inner acrosomal membrane and equatorial segment [13].
  • In conclusion, our present data suggest that human SP-10, expressed on the equatorial region of acrosome-reacted sperm, indeed mediates sperm-oolemma binding in a beta(1) integrin-independent manner, but not sperm-zona binding [4].
  • The interaction of the human acrosomal protein SP-10 with the acrosomal membranes was analyzed by the ability of Triton X-114 (TX-114) and other agents to release SP-10 from the acrosome [14].
  • Sequential treatments of human sperm with various agents showed that repeated washes with TX-114 or 1.5 M NaCl had little or no effect on TX-114-resistant SP-10, whereas treatment with a chaotropic salt (150 mM sodium thiocyanate) and buffers at pH extremes (pH 2.0 and 10.0) completely released this pool of SP-10 from the acrosome [14].
  • Low-temperature post-embed labeling of thin sections with wheat germ agglutinin and monoclonal antibody J18/2 show concentrations of label within the acrosomal vesicle of Strongylocentrotus purpuratus sperm, suggesting the presence of an intracellular storage site for the 210 kDa glycoprotein [15].

Regulatory relationships of ACRV1


Other interactions of ACRV1


Analytical, diagnostic and therapeutic context of ACRV1


  1. Cloning and sequencing of cDNAs coding for the human intra-acrosomal antigen SP-10. Wright, R.M., John, E., Klotz, K., Flickinger, C.J., Herr, J.C. Biol. Reprod. (1990) [Pubmed]
  2. Synthetic peptides containing T and B cell epitopes from human immunodeficiency virus envelope gp120 induce anti-HIV proliferative responses and high titers of neutralizing antibodies in rhesus monkeys. Hart, M.K., Palker, T.J., Matthews, T.J., Langlois, A.J., Lerche, N.W., Martin, M.E., Scearce, R.M., McDanal, C., Bolognesi, D.P., Haynes, B.F. J. Immunol. (1990) [Pubmed]
  3. Polyvalent human immunodeficiency virus synthetic immunogen comprised of envelope gp120 T helper cell sites and B cell neutralization epitopes. Palker, T.J., Matthews, T.J., Langlois, A., Tanner, M.E., Martin, M.E., Scearce, R.M., Kim, J.E., Berzofsky, J.A., Bolognesi, D.P., Haynes, B.F. J. Immunol. (1989) [Pubmed]
  4. A monoclonal antibody to human SP-10 inhibits in vitro the binding of human sperm to hamster oolemma but not to human Zona pellucida. Hamatani, T., Tanabe, K., Kamei, K., Sakai, N., Yamamoto, Y., Yoshimura, Y. Biol. Reprod. (2000) [Pubmed]
  5. suREJ3, a polycystin-1 protein, is cleaved at the GPS domain and localizes to the acrosomal region of sea urchin sperm. Mengerink, K.J., Moy, G.W., Vacquier, V.D. J. Biol. Chem. (2002) [Pubmed]
  6. Increased association of synaptosome-associated protein of 25 kDa with syntaxin and vesicle-associated membrane protein following acrosomal exocytosis of sea urchin sperm. Schulz, J.R., Sasaki, J.D., Vacquier, V.D. J. Biol. Chem. (1998) [Pubmed]
  7. The benzamide derivative N-[1-(7-tert-Butyl-1H-indol-3-ylmethyl)-2-(4-cyclopropanecarbonyl-3-methyl-piperazin-1-yl)-2-oxo-ethyl]-4-nitro-benzamide (SP-10) reduces HIV-1 infectivity in vitro by modifying actin dynamics. Xu, J., Lecanu, L., Tan, M., Yao, W., Greeson, J., Papadopoulos, V. Antivir. Chem. Chemother. (2006) [Pubmed]
  8. Effect of delayed toxicity of chemical barriers to control Argentine ants (Hymenoptera: Formicidae). Soeprono, A.M., Rust, M.K. J. Econ. Entomol. (2004) [Pubmed]
  9. Refinement of the localization of the gene for human intraacrosomal protein SP-10 (ACRV1) to the junction of bands q23-->q24 of chromosome 11 by nonisotopic in situ hybridization. Golden, W.L., von Kap-Herr, C., Kurth, B., Wright, R.M., Flickinger, C.J., Eddy, R., Shows, T., Herr, J.C. Genomics (1993) [Pubmed]
  10. Cloning and characterization of the gene coding for the human acrosomal protein SP-10. Wright, R.M., Suri, A.K., Kornreich, B., Flickinger, C.J., Herr, J.C. Biol. Reprod. (1993) [Pubmed]
  11. Human SP-10: acrosomal distribution, processing, and fate after the acrosome reaction. Foster, J.A., Klotz, K.L., Flickinger, C.J., Thomas, T.S., Wright, R.M., Castillo, J.R., Herr, J.C. Biol. Reprod. (1994) [Pubmed]
  12. Purification and microsequencing of the intra-acrosomal protein SP-10. Evidence that SP-10 heterogeneity results from endoproteolytic processes. Herr, J.C., Klotz, K., Shannon, J., Wright, R.M., Flickinger, C.J. Biol. Reprod. (1992) [Pubmed]
  13. Biochemical and morphological characterization of the intra-acrosomal antigen SP-10 from human sperm. Herr, J.C., Flickinger, C.J., Homyk, M., Klotz, K., John, E. Biol. Reprod. (1990) [Pubmed]
  14. Interactions of human sperm acrosomal protein SP-10 with the acrosomal membranes. Foster, J.A., Herr, J.C. Biol. Reprod. (1992) [Pubmed]
  15. Localization of wheat germ agglutinin and antibody binding sites on the plasma membranes of sea urchin sperm heads as revealed by label-fracture and fracture-flip. Shen, R.L., Ward, R.D., Pinto da Silva, P., Nishioka, D. Mol. Reprod. Dev. (1991) [Pubmed]
  16. Positive selection in the carbohydrate recognition domains of sea urchin sperm receptor for egg jelly (suREJ) proteins. Mah, S.A., Swanson, W.J., Vacquier, V.D. Mol. Biol. Evol. (2005) [Pubmed]
  17. Production in Escherichia coli, purification and immunogenicity of acrosomal protein SP-10, a candidate contraceptive vaccine. Reddi, P.P., Castillo, J.R., Klotz, K., Flickinger, C.J., Herr, J.C. Gene (1994) [Pubmed]
  18. Identification of human acrosomal antigen SP-10 in primates and pigs. Herr, J.C., Wright, R.M., John, E., Foster, J., Kays, T., Flickinger, C.J. Biol. Reprod. (1990) [Pubmed]
  19. Immature spermatids are not prevalent in semen from men who are receiving androgen-based contraceptive regimens. Zhengwei, Y., Wreford, N.G., Bremner, W.J., Matsumoto, A.M., Anawalt, B.A., McLachlan, R.I. Fertil. Steril. (1998) [Pubmed]
  20. Differential diagnosis of immature germ cells in semen utilizing monoclonal antibody MHS-10 to the intra-acrosomal antigen SP-10. Homyk, M., Anderson, D.J., Wolff, H., Herr, J.C. Fertil. Steril. (1990) [Pubmed]
  21. cis-requirement for the maintenance of round spermatid-specific transcription. Acharya, K.K., Govind, C.K., Shore, A.N., Stoler, M.H., Reddi, P.P. Dev. Biol. (2006) [Pubmed]
  22. An antigenically related polypeptide family is a major structural constituent of a stable acrosomal matrix assembly in bovine spermatozoa. Olson, G.E., Winfrey, V.P., Neff, J.C., Lukas, T.J., NagDas, S.K. Biol. Reprod. (1997) [Pubmed]
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