Premium
PilC of pathogenic Neisseria is associated with the bacterial cell surface
Author(s) -
Rahman Motiur,
Källström Helena,
Normark Staffan,
Jonsson AnnBeth
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.4601823.x
Subject(s) - pilus , neisseria meningitidis , biology , neisseria , microbiology and biotechnology , pilin , glycosylation , fimbriae proteins , mutant , bacterial genetics , fimbria , bacterial outer membrane , bacteria , gene , genetics , virulence , escherichia coli
Adherence of pathogenic Neisseria to target host cells is mediated by pili. PilC1 and PilC2 are two high‐molecular‐weight proteins involved in pilus assembly and cellular adherence functions of the pili. Inactivation of pilC1 or pilC2 in N. meningitidis resulted in clones that expressed the same number of pili as the parent, contained no alterations in pilE and showed no detectable differences in PilE glycosylation. However, the PilC2 + pilC1 − mutant showed much reduced adherence to target cells, indicating that production of PilC1 is essential for pilus‐mediated adherence. To study further the functional differences between the meningococcal pilC genes, we determined the complete nucleotide sequence of pilC1 and pilC2 of N. meningitidis . Alignment of six PilC sequences demonstrated that PilC is composed of both conserved and variable regions. By immunogold labelling of bacterial sections we showed that PilC is present in the membranes of both piliated and non‐piliated bacteria. Further, we demonstrated that PilC is associated with the bacterial cell surface.