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    This article has been cited by the following publications. This list is generated based on data provided by CrossRef.
    Conraths, Franz J. Hirzmann, Jörg Hobom, Gerd and Zahner, Horst 1997. Expression of the Microfilarial Sheath Protein 2 (shp2) of the Filarial ParasitesLitomosoides sigmodontisandBrugia malayi. Experimental Parasitology, Vol. 85, Issue. 3, p. 241.
    Hintz, Martin Kasper, Martin Stahl, Bernd Geyer, Rudolf Kalinowski, Hans-Otto Karas, Michael Kühnhardt, Siegfried Schott, Hans-Henning Conraths, Franz Zahner, Horst and Stirm, Stephan 1996. Dimethylaminoethanol is a major component of the Litomosoides carinii microfilarial sheath. Molecular and Biochemical Parasitology, Vol. 76, Issue. 1-2, p. 325.
    Zahner, H. Hobom, G. and Stirm, S. 1995. The microfilarial sheath and its proteins. Parasitology Today, Vol. 11, Issue. 3, p. 116.
    Schares, G. Schützle, B. Zahner, H. and Conraths, F. J. 1994. Surface antigens of Litomosoides carinii microfilariae: agglutinating antibodies react with sheath components of 40 and 120 kiloDalton molecular mass. Parasitology, Vol. 109, Issue. 01, p. 73.
    Hintz, Martin Hirzmann, Jörg Hobom, Gerd Linder, Dietmar Lottspeich, Friedrich Schott, Hans-Henning Conraths, Franz J. Zahner, Horst and Stirm, Stephan 1994. Litomosoides carinii microfilarial sheaths: Partial amino-acid sequences of several major polypeptide constituents. Molecular and Biochemical Parasitology, Vol. 67, Issue. 1, p. 69.
    Conraths, Franz J. Schützle, Birgit Schares, Gereon Christ, Heike Hobom, Gerd and Zahner, Horst 1993. The gene coding for the major sheath protein of Litomosoides carinii microfilariae, gp22, is transcribed in oocytes and embryonic cells. Molecular and Biochemical Parasitology, Vol. 60, Issue. 1, p. 111.
    Christ, Heike Hirzmann, Jörg Conraths, Franz Zahner, Horst Stirm, Stephan and Hobom, Gerd 1992. Trans-splicing, of an early embryo mRNA in Litomosoides carinii, coding for the major microfilarial sheath protein gp22. Gene, Vol. 121, Issue. 2, p. 219.
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A major Litomosoides carinii microfilarial sheath glycoprotein (gp22): amino terminal sequence and immunological studies with corresponding synthetic peptides

  • G. Bardehle (a1), F. J. Conraths (a2), F. Fahrenholz (a3), M. Hintz (a1), D. Linder (a1), G. Schares (a2), H.-H. Schott (a1), B. Schützle (a3), S. Stirm (a1), W. Stüber (a4) and H. Zahner (a2)...
Extract

The major glycoprotein of the sheath of Litomosoides carinii microfilariae (gp22) was analysed for its amino acid and amino sugar composition. It is rich in proline, glutamine/glutamic acid and glycine and contains (N-acetyl)galactosamine. The N-terminal amino acid sequence was determined up to position 37. It consists of a group of 6 repeats of the pentapeptide sequence methionine-glycine-proline-glutamine-proline with two minor modifications in repeats 3–6, while the first two repeats follow the general pattern more loosely. Identical N-terminal amino acid sequences were found in at least two other sheath polypeptides (33 kDa, 39 kDa). Antisera prepared against 3 overlapping synthetic peptides corresponding to the amino terminus of gp22 recognized different epitopes. They all reacted with identical patterns of sheath polypeptides. The antisera failed to recognize antigens of 4th-stage larvae of L. carinii. In contrast, cross-reacting epitopes were detected in other parasite stages. Antisera reacted with material surrounding embryos and microfilariae in the uterus of females, and caused patchy fluorescence on the sheath of blood-derived and in vitro-released microfilariae.

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References
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