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Lectin binding sites on head structures of the spermatid and spermatozoon of the mosquito Culex quinquefasciatus (Diptera, Culicidae)

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Abstract

The presence of intranuclear and acrosomal lectin binding sites in spermatids and spermatozoa of the mosquito Culex quinquefasciatus was analysed. Direct and indirect lectin-gold techniques were used on LR White-embedded cells. The nuclear compartment was the structure most intensely labelled. Early spermatid nucleus showed moderate labelling for peanut agglutinin (PNA), Griffonia simplicifolia IB4 (GS-IB4) and Ricinus communis agglutinin (RCA), and light labelling for the other lectins tested. The sperm nucleus was intensely labelled by all lectins. The acrosome, an enzyme-containing structure, was labelled by some lectins. The anterior acrosomal region was labelled by PNA, while the proximal acrosomal region was labelled by PNA and G. simplicifolia II (GS II) lectins, and showed the presence of fucose residues with the use of Ulex europaeus I (UEA-I) lectin. The spermatozoa stored in the spermatheca showed the same pattern of labelling as that observed in spermatozoa localized in testis and seminal vesicles for all lectins tested. Carbohydrate residues in the nuclear compartment may be involved with the process of chromatin condensation. In the acrosomal region these residues may play a role in the process of spermoocyte interaction.

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References

  • Ahluwalia B, Farshori P, Jamuar M, Baccetti B, Anderson WA (1990) Specific localization of lectins in boar and bull spermatozoa. J Submicrosc Cytol Pathol 22:53–62

    Google Scholar 

  • Aketa K (1975) Physiological studies on the sperm surface component responsible for sperm-egg binding in sea urchin fertilization. II. Effect of Concanavalin A on the fertilizing capacity of sperm. Expt Cell Res 90:56–62

    Google Scholar 

  • Alroy J, Ucci AA, Pereira MEA (1984) Lectins as histochemical probes for specific carbohydrate residues. In: DeLellis RA (ed) Advances in immunohistochemistry. Masson, New York, pp 67–88

    Google Scholar 

  • Bendayan M, Benhamou N, Desjardins M (1990) Ultrastructural distribution of lectin-binding sites in the glomerular wall of streptozotocin-induced diabetic rats. J Submicrosc Cytol Pathol 22:173–184

    Google Scholar 

  • Berryman MA, Rodewald RD (1990) An enhanced method for post-embedding immunocytochemical staining which preserves cell membranes. J Histochem Cytochem 38:159–170

    Google Scholar 

  • Ertl C, Wrobel KH (1992) Distribution of sugar residues in the bovine testis during postnatal ontogenesis demonstrated with lectin-horseradish peroxidase conjugates. Histochemistry 97:161–171

    Google Scholar 

  • Fakan S, Nobis P (1987) Ultrastructural localization of transcription sites and of RNA distribution during the cell cycle of synchronized CHO cell. Exp Cell Res 113:327–337

    Google Scholar 

  • Ferraro A, Antonilli L, D'Ermo M, Eufemi M, Rosei MA, Spoto G (1988) Glycoprotein distribution in nonhistone chromatin proteins from pig liver. Ital J Biochem 37:213–218

    Google Scholar 

  • Friess AE, Toepter-Petersen E, Nguyen H, Schill WB (1987) Electron microscopic localization of a fucose-binding protein in acrosome reacted boar spermatozoa by the fucosyl-peroxidase gold method. Histochemistry 86:297–303

    Google Scholar 

  • Furukawa K, Terayama H (1979) Pattern of glycosaminoglycans and glycoproteins associated with nuclei of regenerating liver of rat. Biochem Biophys Acta 585:575–588

    Google Scholar 

  • Gallo J, Escalier D, Grellier P, Précigout E, Albert M, David G, Schrével J (1991) Characterization of a monoclonal antibody to human proacrosin and its use in acrosomal status evaluation. J Histochem Cytochem 39:273–282

    Google Scholar 

  • Hart GW, Holt GD, Haltiwanger RS (1988) Nuclear and cytoplasmic glycosylation: novel saccharide linkages in unexpected places. Trends Biochem Sci 13:380–384

    Google Scholar 

  • Hart GW, Haltiwanger RS, Holt GD, Kelly WG (1989) Glycosylation in the nucleus and cytoplasm. Annu Rev Biochem 58:841–874

    Google Scholar 

  • Hubert J, Séve AP, Facy P, Monsigny M (1989) Are nuclear lectins and nuclear glycoproteins involved in the modulation of nuclear functions? Cell Differ Dev 27:69–81

    Google Scholar 

  • Kan FWK, Pinto da Silva P (1986) Preferential association of glycoproteins to the euchromatin regions of cross-fractured nuclei is revealed by fracture-label. J Cell Biol 102:576–586

    Google Scholar 

  • Kinoshita S, Yoshii K, Tonegawa Y (1988) Specific binding of lectins with the nucleus of the sea urchin embryo and changes in the lectin affinity of the embryonic chromatin during the course of development. Expt Cell Res 175:148–157

    Google Scholar 

  • Levy-Wilson B (1983) Glycosylation, ADP-ribosylation, and methylation of Tetrahymena histones. Biochemistry 22:484–489

    Google Scholar 

  • Loir M, Lanneau M (1984) Structural function of the basic nuclear proteins in ram spermatids. J Ultrastruct Res 86:262–276

    Google Scholar 

  • Londono I, Bendayan M (1987) Ultrastructural localization of mannoside residues on tissue sections: comparative evaluation of the enzyme-gold and the lectin-gold approaches. Eur J Cell Biol 45:88–96

    Google Scholar 

  • Martinage A, Gusse M, Bélaiche D, Sautiere PM, Chevaillier P (1985) Amino acid sequence of a cysteine-rich, arginine-rich sperm protamine of the dog-fish Scylliorhinus caniculus. Biochem Biophys Acta 831:172–178

    Google Scholar 

  • Martinez-Menárguez JA, Ballesta J, Avilés M, Castells MT, Madrid JF (1992) Cytochemical characterization of glycoproteins in the developing acrosome of rats: an ultrastructural study using lectin histochemistry, enzymes and chemical deglycosylation. Histochemistry 97:439–449

    Google Scholar 

  • McMaster-Kayer R, Kaye JS (1976) Basic protein changes during the final stages of sperm maturation in the house cricket. Expt Cell Res 97:378–386

    Google Scholar 

  • Mello MLS (1987) Nuclear cytochemistry and polarization microscopy of the spermatozoa of Triatoma infestans Klug. Z Mikrosk Anat Forsch 101:245–250

    Google Scholar 

  • Nicolson GL (1974) The interaction of lectins with animal cell surfaces. Int Rev Cytol 39:89–190

    Google Scholar 

  • Nicolson GL, Yanagimachi R (1972) Terminal saccharides on sperm plasma membranes: identification by specific agglutinins. Science 1977:276–279

    Google Scholar 

  • Perotti ME, Riva A (1988) Concanavalin A binding sites on the surface of Drosophila melanogaster sperm: a fluorescence and ultrastructural study. J Ultrastruct Mol Struct Res 100:173–182

    Google Scholar 

  • Quagio-Grassiotto I, Dolder H (1988) The basic nucleoprotein E-PTA reaction during spermiogenesis of Ceratitis capitata (Diptera, Tephritidae). Cytobios 53:153–158

    Google Scholar 

  • Rizzo WB, Bustin M (1977) Lectins as probes of chromatin structure. J Biol Chem 252:7062–7067

    Google Scholar 

  • Roth J (1983) Application of lectin-gold complexes for electron microscopic localization of glycoconjugates on thin sections. J Histochem Cytochem 31:987–999

    Google Scholar 

  • Seve AP, Hubert J, Bouvier D, Masson C, Geraud G, Bouteille M (1984) In situ distribution in different cell types of nuclear glycoconjugates detected by two lectins. J Submicrosc Cytol 16:631–641

    Google Scholar 

  • Sharon N (1984) Glycoproteins. Trends Biochem Sci 9:198–202

    Google Scholar 

  • Stein GS, Roberts RM, Davis JL, Head WJ, Stein JL, Thrall CL, Vanneen J, Welch DW (1975) Are glycoproteins and glycosaminoglycans components of the eucaryotic genome? Nature 258:639–641

    Google Scholar 

  • Tesarik J, Drahorad J, Testart J, Mendoza C (1990) Acrosin activation follows its surface exposure and precedes membrane fusion in human sperm acrosome reaction. Development 110:391–400

    Google Scholar 

  • Topfer-Petersen E, Calvete J, Schafer W, Henschen A (1990) Complete localization of the disulfide bridges and glycosylation sites in boar sperm acrosin. FEBS Lett 275:139–142

    Google Scholar 

  • Vannier-Santos MA, Saraiva EMB, De Souza W (1991) Nuclear and cytoplasmic lectin binding sites in promastigotes of Leishmania. J Histochem Cytochem 39:793–800

    Google Scholar 

  • Weisbrod S, Groudine M, Weintraub H (1980) Interaction of HMG 14 and 17 with actively transcribed genes. Cell 19:289–301

    Google Scholar 

  • Yanagimachi R (1988) Mammalian fertilization. In: Knobil E, Neill J (eds) The physiology of reproduction. Raven Press, New York, pp 135–185

    Google Scholar 

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Báo, S.N., de Souza, W. Lectin binding sites on head structures of the spermatid and spermatozoon of the mosquito Culex quinquefasciatus (Diptera, Culicidae). Histochemistry 98, 365–371 (1992). https://doi.org/10.1007/BF00271072

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