Molecular basis of the length variation in the N-terminal part of Mycoplasma synoviae hemagglutinin.

@article{Benina2001MolecularBO,
  title={Molecular basis of the length variation in the N-terminal part of Mycoplasma synoviae hemagglutinin.},
  author={Du{\vs}an Ben{\vc}ina and M Drobnic-Valic and Simon Horvat and Mojca Narat and Stanley H. Kleven and Peter Dov{\vc}},
  journal={FEMS microbiology letters},
  year={2001},
  volume={203 1},
  pages={
          115-23
        }
}
Mycoplasma synoviae is a major avian pathogen that synthesizes hemagglutinin VlhA, an abundant immunodominant surface lipoprotein. In most M. synoviae strains, the VlhA protein cleaves into the N-terminal part, a lipoprotein MSPB, and a C-terminal part MSPA, which mediates binding to erythrocytes. VlhA is encoded by the vlhA gene of which the 5'-end is present in the genome as a single copy, which does not change its sequence during recombination of the vlhA gene with pseudogenes. In this study… CONTINUE READING

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