Antigenic relationships of transferrin-binding proteins from Neisseria meningitidis, N. gonorrhoeae and Haemophilus influenzae : cross-reactivity of antibodies to NH2-terminal peptides

• Published in: FEMS microbiology letters 1993-05, Vol.109 (1), p.85-91
• Main Authors: GRIFFITHS, E, STEVENSON, P, BYFIELD, P, ALA'ALDEEN, D. A, BORRIELLO, S. P, HOLLAND, J, PARSONS, T, WILLIAMS, P
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Antibodies, Bacterial; Antigens, Bacterial - genetics; Bacterial Proteins - genetics; Bacterial Proteins - immunology; Bacteriology; Biological and medical sciences; Carrier Proteins - genetics; Carrier Proteins - immunology; Conserved Sequence; Cross Reactions; Fundamental and applied biological sciences. Psychology; Haemophilus influenzae - genetics; Haemophilus influenzae - immunology; Haemophilus influenzae - metabolism; Iron-Binding Proteins; Microbiology; Molecular Sequence Data; Morphology, structure, chemical composition; Neisseria gonorrhoeae - genetics; Neisseria gonorrhoeae - immunology; Neisseria gonorrhoeae - metabolism; Neisseria meningitidis - genetics; Neisseria meningitidis - immunology; Neisseria meningitidis - metabolism; Peptide Fragments - genetics; Peptide Fragments - immunology; Rabbits; Sequence Homology, Amino Acid; Species Specificity; Transferrin - metabolism; Transferrin-Binding Proteins
• ISSN: 0378-1097; 1574-6968

The NH2-terminal amino sequence through the first 20 amino acids was obtained for transferrin-binding protein (TBP)1 from three strains of Neisseria meningitidis. These were identical except for a glutamine to a glycine substitution at residue 6 in one case. The sequences of the NH2-terminal 20 amino acids of TBP2 from the same three strains were also determined; one TBP2 had a M(r) of 68,000 and the other two of 78,000. Sequences were identical up to residue 13 in all three proteins. Peptides based on the NH2-terminal sequences of TBP1 and 2 were synthesized, linked to Keyhole Limpet haemocyanin and used to raise antibodies in rabbits. Anti-peptide antibodies cross-reacted on immunoblotting with the respective TBPs from all meningococcal strains tested, as well as with those from N. gonorrhoeae, suggesting that the NH2-terminals of these proteins are well conserved in the Neisseria. Neither anti-peptide serum reacted with the analogous TBP1 and 2 from Haemophilus influenzae, although common epitopes have previously been shown to exist.