Open AccessN‐terminal amino acid sequence of the Borrelia burgdorferi flagellin
Author(s) -
Gβmann G.S.,
Deutzmann R.,
Vogt A.,
Göbel U.B.
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03427.x
Subject(s) - flagellin , borrelia burgdorferi , microbiology and biotechnology , peptide sequence , chemistry , terminal (telecommunication) , sequence (biology) , biology , bacteria , biochemistry , genetics , gene , antibody , computer science , telecommunications
The 41 kDa flagellar protein of Borrelia burgdorferi appears to be an immunodominant antigen producing an early and strong response in most, if not all, individuals during infection in humans. It would represent a very good antigen for serodiagnosis of Lyme disease, if its crossreactivity with flagella of other bacteria was low. To gain information on this point we isolated the B. burgdorferi flagellin by preparative two‐dimensional electrophoresis for N‐terminal amino acid analysis. By comparing the N‐terminal amino acid sequences of flagellar proteins from other eubacteria we found that the first six out of twenty nine amino acids were identical to the Treponema pallidum and Treponema phagedenis ‘class B’ flagellins. All 29 N‐terminal residues exhibited a moderate inter‐genus homology (44–55%), in contrast to the high degree (67–95%) of inter‐species conservation of the treponemal ‘class B’ flagellar N‐terminal sequences. There was little similarity to other flagellins except the B. subtilis flagellar protein.