The variable adherence-associated (Vaa) adhesin of the opportunistic human
pathogen Mycoplasma hominis is a surface-exposed, membrane-associated prote
in 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 -heli
cal content of similar to 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 rec
ombinant proteins corresponding to the N- or C-terminal parts of the shorte
st one-cassette form of the protein were consistent with the hypothesis of
two distinct coiled-coil regions. The one-cassette Vaa monomer appears to b
e 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 inte
rpreted in terms of the topological organization of the Vaa protein indicat
ing the localization of the adherence-mediating structure.