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Protein Science (2001), 10:2577-2586.
Copyright © 2001 The Protein Society

Molecular design of Mycoplasma hominis Vaa adhesin

Thomas Boesen1, Natalya U. Fedosova2, Morten Kjeldgaard3, Svend Birkelund1 and Gunna Christiansen1

1 Department of Medical Microbiology and Immunology, University of Aarhus, DK-8000 Aarhus C, Denmark
2 Department of Biophysics, University of Aarhus, DK-8000 Aarhus C, Denmark
3 Department of Molecular and Structural Biology, University of Aarhus, DK-8000 Aarhus C, Denmark

Reprint requests to: Dr. Thomas Boesen, Department of Medical Microbiology, The Bartholin Building, University of Aarhus, DK-8000 Aarhus C, Denmark; e-mail: tboesen{at}biobase.dk; fax: 45-8619-6128.

The variable adherence-associated (Vaa) adhesin of the opportunistic human pathogen Mycoplasma hominis is a surface-exposed, membrane-associated protein involved in the attachment of the bacterium to host cells. The molecular masses of recombinant 1 and 2 cassette forms of the protein determined by a light-scattering (LS) method were 23.9 kD and 36.5 kD, respectively, and corresponded to their monomeric forms. Circular dichroism (CD) spectroscopy of the full-length forms indicated that the Vaa protein has an {alpha}-helical content of ~80%. Sequence analysis indicates the presence of coiled-coil domains in both the conserved N-terminal and antigenic variable C-terminal part of the Vaa adhesin. Experimental results obtained with recombinant proteins corresponding to the N- or C-terminal parts of the shortest one-cassette form of the protein were consistent with the hypothesis of two distinct coiled-coil regions. The one-cassette Vaa monomer appears to be an elongated protein with a axial shape ratio of 1:10. Analysis of a two-cassette Vaa type reveals a similar axial shape ratio. The results are interpreted in terms of the topological organization of the Vaa protein indicating the localization of the adherence-mediating structure.

Keywords: Coiled coil; bacterial surface protein; Mycoplasma hominis; Vaa; adhesin


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