Light and electron microscopic immunolocalization of sperm proteins identified by monoclonal antibodies from the World Health Organization Task Force on Sperm Antigens

Homyk, Mona; Herr, John C.

doi:10.1016/0165-0378(92)90046-7

Cited by 14 publications

(5 citation statements)

References 21 publications

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“…MAbs S69 and S70 recognize human 68-kD and 54-51-kD major FS polypeptides (Beecher et al 1993) and AJ-FS1 multiple bands ranging between 97 and 28 kD (Jassim and Chen 1994). Unlike MAb 4F7, AJ-FS1 (Jassim and Chen 1994) and S69 (Beecher et al 1993;Homyk and Herr 1992) bind only to the outer side of the FS. The RT97 anti-neurofilament antibody recognizes a single 97-kD peptide of the human FS, showing that the human FS shares an epitope common to anti-200-kD neurofilament (Jassim et al , 1992Jassim 1991).…”

Section: Discussionmentioning

confidence: 99%

Immunochemical Characterization of a Human Sperm Fibrous Sheath Protein, Its Developmental Expression Pattern, and Morphogenetic Relationships with Actin

Escalier

Gallo²,

Schrével³

1997

J Histochem Cytochem.

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SUMMARY Among the monoclonal antibodies (MAbs) prepared against human sperm extracts, MAb 4F7 was found to be specific to the human and Macaca fascicularis sperm cytoskeletal fibrous sheath (FS). In Western blotting, MAb 4F7 stains a doublet of polypeptides of about M r 95 ϫ 10 3 in extracts of human sperm cells. These polypeptides are not recognized by the KL1 anti-cytokeratin MAb, nor by the MAbs known to bind to the carboxy terminal (IFA) and to the amino terminal (ME101) rod domain of intermediate filaments.Sequential extraction procedures shows that the FS polypeptides recognized by MAb 4F7 are exposed after treatment with 8 M urea. 4F7 immunoreactivity is lost after treatment with high ionic solutions (NaCl, KCl, KI). Immunogold electron microscopy reveals that this protein is present throughout the FS. This FS antigenic determinant first accumulates in an FS proximal body in late spermatids, then in granules extending distally along the flagellum. Staining of spermatozoa with flagellar dysgenesis reveals that this FS protein colocalizes with actin no matter what the location of their abnormal assembly. These data suggest that the transient microtubule-like spindle-shaped body of as yet unknown function could be involved in FS protein deposition and that the assembly of the FS and actin could be under the control of some common morphogenetical factor(s). MAb 4F7 should allow further investigations of this peri-axonemal structure in both normal and pathological conditions. (J Histochem Cytochem 45:909-922, 1997)

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Section: Discussionmentioning

confidence: 99%

Immunochemical Characterization of a Human Sperm Fibrous Sheath Protein, Its Developmental Expression Pattern, and Morphogenetic Relationships with Actin

Escalier

Gallo²,

Schrével³

1997

J Histochem Cytochem.

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“…Immunofluorescence of viable spermatozoa confirmed this localization and immunoelectron microscopy detected S19 immunoreactivity exclusively on the sperm surface. 75,76 In the sperm immobilization test, 77 the S19 mAb demonstrated a dose-dependent immobilizing effect on human spermatozoa in the presence of complement indicating that the binding of antibody to SAGA-1 carbohydrate epitopes has a complement-dependent, cytotoxic effect on human spermatozoa. 72 The World Health Organization-sponsored workshops on antisperm mAbs reported that the S19 mAb also impeded sperm penetration of cervical mucus, inhibited the penetration of hamster ova by human spermatozoa, and inhibited mouse in 6itro fertilization.…”

Section: The Human H6-3c4 Mab From An Infertile Womanmentioning

confidence: 99%

Anti‐Sperm Antibodies from Infertile Patients and their Cognate Sperm Antigens: A Review. Identity Between SAGA‐1, the H6‐3C4 Antigen, and CD52

Diekman

Norton

Westbrook

et al. 2000

American J Rep Immunol

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“…The S19 epitope has been localized over the entire human sperm surface by immunofluorescence and ultrastructural analysis [21]. In the present study, the S19 epitope localized to the entire surface of chimpanzee spermatozoa, rendering cells susceptible to agglutination on exposure to the anti-SAGA-1 S19 mAb.…”

Section: Discussionmentioning

confidence: 97%

Analysis of a Human Sperm CD52 Glycoform in Primates: Identification of an Animal Model for Immunocontraceptive Vaccine Development1

McCauley¹,

Kurth

Norton

et al. 2002

Biology of Reproduction

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Sperm agglutination antigen-1 (SAGA-1) is a human male reproductive tract glycoform of CD52. Unique modification of CD52 N-linked oligosaccharide chains in the epididymis and vas deferens results in the appearance of a carbohydrate epitope that is localized over the entire surface of human spermatozoa. SAGA-1 was characterized by the sperm-inhibitory murine monoclonal antibody (mAb) S19, and it is the target antigen of a human mAb (H6-3C4) associated with antibody-mediated infertility. Collectively, sperm surface localization, antibody inhibition of sperm function, and potential reproductive-tissue specificity identify SAGA-1 as an attractive candidate contraceptive immunogen. To establish an animal model for the study of SAGA-1 in immunologic infertility and immunocontraceptive development, we investigated the appearance of the S19 carbohydrate epitope in nonhuman primates. The S19 mAb demonstrated little to no immunoreactivity by Western blot analysis with protein extracts of spermatozoa from the baboon, marmoset, bonnet, cynomolgus, and pigtailed macaques. Immunohistochemical analysis identified CD52 in the bonnet monkey epididymis; however, the N-linked carbohydrate moiety recognized by the S19 mAb, and unique to SAGA-1, was absent. In contrast, the S19 carbohydrate epitope was identified in chimpanzee sperm extracts by Western blot analysis and in chimpanzee epididymal tissue sections by immunohistochemical analysis, indicating that it is conserved in this close relative of the human. Chimpanzee testis, seminal vesicle, and prostate do not express the S19 epitope. Although anti-CD52 immunoreactivity was identified in the spleen, the carbohydrate moiety recognized by the S19 mAb was absent, corroborating data in the human that demonstrated tissue-specific glycosylation of sperm CD52. Immunofluorescent analysis indicated that the chimpanzee homologue of sperm CD52 was present over the entire spermatozoon. In addition, the S19 mAb agglutinated chimpanzee spermatozoa in a manner similar to the effect observed on human spermatozoa. These data indicate that the distinctive carbohydrate moiety of human sperm CD52 is present in the chimpanzee, and they identify the chimpanzee as the most appropriate primate model to study the potential of this unique CD52 glycoform as a contraceptive immunogen.

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Light and electron microscopic immunolocalization of sperm proteins identified by monoclonal antibodies from the World Health Organization Task Force on Sperm Antigens

Cited by 14 publications

References 21 publications

Immunochemical Characterization of a Human Sperm Fibrous Sheath Protein, Its Developmental Expression Pattern, and Morphogenetic Relationships with Actin

Immunochemical Characterization of a Human Sperm Fibrous Sheath Protein, Its Developmental Expression Pattern, and Morphogenetic Relationships with Actin

Anti‐Sperm Antibodies from Infertile Patients and their Cognate Sperm Antigens: A Review. Identity Between SAGA‐1, the H6‐3C4 Antigen, and CD52

Analysis of a Human Sperm CD52 Glycoform in Primates: Identification of an Animal Model for Immunocontraceptive Vaccine Development1

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