Flagellin proteins from several different strains of Pseudomonas pseud
omallei have been isolated and purified to homogeneity by mechanical s
hearing and differential centrifugation techniques. Analysis by sodium
dodecyl sulfate-polyacrylamide gel electrophoresis yielded flagellin
monomer protein hands with an estimated M(r) of 43,400. No lipopolysac
charide contamination of the purified protein preparations was detecta
ble by silver staining of flagellin displayed on polyacrylamide gels a
nd by Western immunoblotting with P. pseudomallei antilipopolysacchari
de monoclonal antibody. NH2-terminal amino acid sequence analysis of t
he flagellin protein of P. pseudomallei 319a revealed significant homo
logy with flagellins from Proteus mirabilis, Bordetella bronchiseptica
, and Pseudomonas aeruginosa PAK. Rabbit polyclonal antiserum raised a
gainst the 319a flagellin protein reacted with 64 of 65 P. pseudomalle
i strains tested. The polyclonal antiserum proved effective in inhibit
ing the motility of these organisms in motility agar plates. Passive i
mmunization studies demonstrated that 319a flagellin-specific antiseru
m was capable of protecting diabetic rats from challenge with a hetero
logous P. pseudomallei strain.