Determination of neutralizing epitopes in variable domains I and IV of the major outer-membrane protein from Chlamydia trachomatis serovar K

Chlamydia trachomatis is a leading cause of sexually transmitted diseases and a number of strategies have been developed to produce vaccines to prevent its transmission

A. Villeneuve

2009

Scholarcy highlights

  • Chlamydia trachomatis is a leading cause of sexually transmitted diseases and a number of strategies have been developed to produce vaccines to prevent its transmission
  • Our data confirmed that a neutralizing epitope is found in VDIV, defined by peptides K12 and K13
  • This epitope is 296TTLNPTIAG304, which has never been reported as a neutralizing epitope of serovar K. Another neutralizing epitope, defined by peptide K2, has been identified in VDI. This epitope is in the same position as 71VAGLEK76, a peptide with neutralizing activity found in serovar A, but they are not identical because antibodies against peptide K2 do not bind to this epitope
  • No neutralizing epitope was found in the two other variable domains
  • Two neutralizing sites, one in variable domain I and one in variable domain IV, were identified in serovar K

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