TY - JOUR
T1 - Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis
T2 - Cell surface polysaccharide as an anchorage for gingipanis
AU - Shoji, Mikio
AU - Ratnayake, Dinath B.
AU - Shi, Yixin
AU - Kadowaki, Tomoko
AU - Yamamoto, Kenji
AU - Yoshimura, Fuminobu
AU - Akamine, Akifumi
AU - Curtis, Michael A.
AU - Nakayama, Koji
PY - 2002/1/1
Y1 - 2002/1/1
N2 - A nonpigmented mutant of Porphyromonas gingivalis was constructed by using transposon mutagenesis. The mutant possessed the transposon DNA at the novel gene porR. Gene targeted mutagenesis revealed that porR was responsible for pigmentation. The porR gene shared similarities with genes of the degT family, the products of which are now considered to be transaminases involved in biosynthesis of sugar portions of cell-surface polysaccharides and aminoglycosides. The porR mutant showed a pleiotropic phenotype: delayed maturation of fimbrillin, preferential presence of Rgp and Kgp proteinases in culture supernatants, and no haemagglutination. The porR mutant had altered phenol extractable polysaccharide compared to the porR+ sibling strain. A mAb, 1B5, that reacts with sugar portions of P. gingivalis cell surface polysaccharide and membrane-type Rgp proteinase showed no reaction with the cell lysates of the porR mutant. These results indicate that porR is involved in biosynthesis of cell surface polysaccharide that may function as an anchorage for Rgp, Kgp, haemagglutinins and the haemoglobin receptor protein.
AB - A nonpigmented mutant of Porphyromonas gingivalis was constructed by using transposon mutagenesis. The mutant possessed the transposon DNA at the novel gene porR. Gene targeted mutagenesis revealed that porR was responsible for pigmentation. The porR gene shared similarities with genes of the degT family, the products of which are now considered to be transaminases involved in biosynthesis of sugar portions of cell-surface polysaccharides and aminoglycosides. The porR mutant showed a pleiotropic phenotype: delayed maturation of fimbrillin, preferential presence of Rgp and Kgp proteinases in culture supernatants, and no haemagglutination. The porR mutant had altered phenol extractable polysaccharide compared to the porR+ sibling strain. A mAb, 1B5, that reacts with sugar portions of P. gingivalis cell surface polysaccharide and membrane-type Rgp proteinase showed no reaction with the cell lysates of the porR mutant. These results indicate that porR is involved in biosynthesis of cell surface polysaccharide that may function as an anchorage for Rgp, Kgp, haemagglutinins and the haemoglobin receptor protein.
KW - Cell surface polysaccharide
KW - Colonial pigmentation
KW - Cysteine proteinases
KW - Fimbrillin maturation
KW - Haemogglutination
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UR - http://www.scopus.com/inward/citedby.url?scp=0036232069&partnerID=8YFLogxK
U2 - 10.1099/00221287-148-4-1183
DO - 10.1099/00221287-148-4-1183
M3 - Article
C2 - 11932462
AN - SCOPUS:0036232069
SN - 1350-0872
VL - 148
SP - 1183
EP - 1191
JO - Microbiology
JF - Microbiology
IS - 4
ER -