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Infection and Immunity, February 2000, p. 680-687, Vol. 68, No. 2
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Epitope Mapping of Immunogenic and Adhesive Structures in Repetitive Domains of Mycoplasma bovis Variable Surface Lipoproteins

K. Sachse,1,* J. H. Helbig,2 I. Lysnyansky,3 C. Grajetzki,1 W. Müller,1 E. Jacobs,2 and D. Yogev3

Division 4, Federal Institute for Health Protection of Consumers and Veterinary Medicine (BgVV), 07743 Jena,1 and Institut für Medizinische Mikrobiologie und Hygiene, Technische Universität Dresden, 01307 Dresden,2 Germany, and Department of Membrane and Ultrastructure Research, Hadassah Medical School, The Hebrew University, Jerusalem 91120, Israel3

Received 27 July 1999/Returned for modification 13 September 1999/Accepted 28 October 1999

The family of variable surface lipoproteins (Vsps) of the bovine pathogen Mycoplasma bovis includes some of the most immunogenic antigens of this microorganism. Vsps were shown to undergo high-frequency phase and size variations and to possess extensive reiterated coding sequences extending from the N-terminal end to the C-terminal end of the Vsp molecule. In the present study, mapping experiments were conducted to detect regions with immunogenicity and/or adhesion sites in repetitive domains of four Vsp antigens of M. bovis, VspA, VspB, VspE, and VspF. In enzyme-linked immunosorbent assay experiments, sera obtained from naturally infected cattle showed antibodies to different repeating peptide units of the Vsps, particularly to units RA1, RA2, RA4.1, RB2.1, RE1, and RF1, all of which were found to contain immunodominant epitopes of three to seven amino acids. Competitive adherence trials revealed that a number of oligopeptides derived from various repeating units of VspA, VspB, VspE, and VspF partially inhibited cytoadhesion of M. bovis PG45 to embryonic bovine lung cells. Consequently, putative adherence sites were identified in the same repeating units (RA1, RA2, RA4.1, RB2.1, RE1, and RF1) and in RF2. The positions and lengths of the antigenic determinants were mostly identical to those of adhesion-mediating sites in all short repeating units, whereas in the considerably longer RF1 unit (84 amino acid residues), there was only one case of identity among four immunogenic epitopes and six adherence sites. The identification of epitopes and adhesive structures in repetitive domains of Vsp molecules is consistent with the highly immunogenic nature observed for several members of the Vsp family and suggests a possible function for these Vsp molecules as complex adherence-mediating regions in pathogenesis.

* Corresponding author. Mailing address: Bundesinstitut für Gesundheitlichen Verbraucherschutz und Veterinärmedizin, Fachbereich 4, Naumburger Str. 96a, 07743 Jena, Germany. Phone: 49-3641-804334. Fax: 49-3641-804228. E-mail: k.sachse{at}bgvv.de.

Infection and Immunity, February 2000, p. 680-687, Vol. 68, No. 2
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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