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Title: Structural studies on flagellins from shape and antigenic variants of Salmonella and Proteus flagella
Author: Baker, Barbara S.
ISNI:       0000 0001 3438 3706
Awarding Body: University of London
Current Institution: Royal Holloway, University of London
Date of Award: 1981
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The primary structures of flagellins from antigenic and shape variants of Salmonella and Proteus flagella were studied. H antigenic differences in Salmonella are related to differences in amino acid composition of the flagellin molecules: peptide differences were observed between thermolytic, and between chymotryptic peptide maps of Salmonella g.... antigenic flagellins. These differences were located on the CNBr A fragments of the flagellins. Homologous CNBr A fragments were almost as effective as homologous flagella as inhibitors of antiserum raised against g.... antigenic flagella, as measured by immobilisation-inhibition and complement fixation-inhibition assays. Thus the H antigenic determinants appear to be located primarily on the CNBr A fragment, although some results suggest that they might extend onto the CNBr B fragment in certain flagellins. The sites of amino acid substitutions in morphological mutants of Salmonella g... antigenic flagellins appear to be located at either the N-terminal (CNBr B) or C-terminal (CNBr C and CNBr D) regions of the flagellin molecule. The C-terminus of the molecule is conserved. Several epsilon-N-methyllysine residues were detected in most of the Salmonella g.... antigenic flagellins analysed and, in fewer numbers, in certain P. morganii flagellins. The absence of E-N-methyllysine residues in flagellins of diverse bacteria was noted. Arginine and tyrosine residues of various bacterial flagellins were differentiated by chemical modification into three groups: residues not accessible to modification; residues accessible in the monomer but not in the polymer; residues which are modified in both the monomer and polymer. Residues belonging to the second group may be implicated in the self-assembly of flagellin subunits into flagellar filaments. Comparison of amino acid sequences of bacterial flagellins indicated sequences of homology at the N- and C-terminal regions of the flagellin molecule. These regions may be essential for the assembly of subunits into functional filaments. The central part of the molecule, however, appears to be a variable region which is exposed in the polymer and predominantly bears the H-antigenic characteristics of the bacterium.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: Botany