The Primary Sequence and Antigenic Structure of Gonococcal Pilin: Approaches Towards a Gonococcal Vaccine

  • Jonathan B. Rothbard
  • Gary K. Schoolnik
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 185)


The complete amino acid sequence of pilin from strain MS11 and the partial sequence of R10 pilin are reported. The protein consists of 159 amino acids and appears to be divided into constant and variable domains. The region of conserved sequence appears to be involved in the polymerization of the molecule and composing the ligand binding site. The carboxyl terminal portion of the molecule contains a thirty amino acid disulfide loop that significantly varies in sequence between the two strains and is postulated to be site of the serological variation in the molecule. The antigenic structure of the molecule was investigated by assaying the binding of antisera engendered by intact pili from strains MS11 and R10 and their two major cyanogen bromide generated fragments, CNBr-2 (residues 9–92) and CNBr-3 (residues 93–159), to synthetic peptides corresponding to the amino acid sequence of MS11 pilin. Two independent, strain specific determinants were found within the disulfide loop. A weakly immunogenic, common determinant was located between residues 48–60. Antisera raised against either MS11 or R10 CNBr-2 bind a separate peptide, residues 69–84. This region is only immunogenic as a fragment, not in the pilus filament. Antisera generated to each of the peptides were assayed for their ability to crossreact with intact pili from both homologous and heterologous strains.


Intact Protein Cyanogen Bromide Strain MS11 Polyclonal Seron Reverse Turn 
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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Jonathan B. Rothbard
    • 1
  • Gary K. Schoolnik
    • 1
  1. 1.Departments of Medicine and Medical MicrobiologyStanford University Medical SchoolStanfordUSA

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