TY - JOUR
T1 - Correlation between molecular size of the surface array protein and morphology and antigenicity of the Campylobacter fetus S layer
AU - Fujimoto, S.
AU - Takade, A.
AU - Amako, K.
AU - Blaser, M. J.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1991
Y1 - 1991
N2 - The correlation between the molecular size of the surface layer protein (S protein) and both structure and antigenicity of the Campylobacter fetus surface layer (S layer) was investigated in several clinical strains and their spontaneous variants which produce S proteins of molecular weights (MW) different from those of the parents. Only three molecular sizes of the S proteins were observed (98, 127, and 149 kDa) in the parental and variant strains. Immunologically, the 98-kDa protein and the 149-kDa protein but not the 127-kDa protein were cross-reactive. Freeze-etching analysis showed that the 98-kDa S protein formed a hexagonal arrangement with a 24-nm center-to-center space and that the S proteins with larger MW (127 or 149 kDa) formed tetragonal ones with an 8-nm center-to-center space. Thus, the MW changes of the S proteins seen in the variant strains were associated with both morphological and antigenic changes in S layer. These observations support the hypothesis that the pattern and antigenicity of the C. fetus S layer is determined by the particular type of S protein. Furthermore, the presence of the two different S layer patterns on a single bacterial cell indicates that multiple S proteins can be produced and expressed in a single cell.
AB - The correlation between the molecular size of the surface layer protein (S protein) and both structure and antigenicity of the Campylobacter fetus surface layer (S layer) was investigated in several clinical strains and their spontaneous variants which produce S proteins of molecular weights (MW) different from those of the parents. Only three molecular sizes of the S proteins were observed (98, 127, and 149 kDa) in the parental and variant strains. Immunologically, the 98-kDa protein and the 149-kDa protein but not the 127-kDa protein were cross-reactive. Freeze-etching analysis showed that the 98-kDa S protein formed a hexagonal arrangement with a 24-nm center-to-center space and that the S proteins with larger MW (127 or 149 kDa) formed tetragonal ones with an 8-nm center-to-center space. Thus, the MW changes of the S proteins seen in the variant strains were associated with both morphological and antigenic changes in S layer. These observations support the hypothesis that the pattern and antigenicity of the C. fetus S layer is determined by the particular type of S protein. Furthermore, the presence of the two different S layer patterns on a single bacterial cell indicates that multiple S proteins can be produced and expressed in a single cell.
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M3 - Article
C2 - 2037362
AN - SCOPUS:0025896407
VL - 59
SP - 2017
EP - 2022
JO - Infection and Immunity
JF - Infection and Immunity
SN - 0019-9567
IS - 6
ER -