TY - JOUR
T1 - Porphyromonas gingivalis proteinases as virulence determinants in progression of periodontal diseases
AU - Kadowaki, Tomoko
AU - Nakayama, Koji
AU - Okamoto, Kuniaki
AU - Abe, Naoko
AU - Baba, Atsuyo
AU - Shi, Yixin
AU - Ratnayake, Dinath B.
AU - Yamamoto, Kenji
PY - 2000/8/1
Y1 - 2000/8/1
N2 - Porphyromonas gingivalis, one of the major causative agents of periodontal diseases, produces large amounts of arginine- and lysine-specific cysteine proteinases in cell-associated and secretory forms, which are now referred to as Arg-gingipain (Rgp) and Lysgingipain (Kgp), respectively. A number of studies have revealed that these proteinases are closely associated with the periodontopathogenesis of this bacterium: destruction of periodontal connective tissues, disruption of host defense mechanisms, and development and maintenance of inflammation in periodontal pockets. With respect to the physiology of the bacterium, Rgp and Kgp are indispensable for it to obtain nutrients from the environment, since it cannot utilize saccharides as carbon/energy sources for growth and totally depends on peptides and amino acids that are provided from environmental proteins by Rgp and Kgp. Furthermore, proteolytic activities of Rgp and Kgp contribute to processing/maturation of various cell-surface proteins of P. gingivalis, such as fimA fimbrilin (a subunit of major fimbriae), 75-kDa protein (a subunit of minor fimbriae), hemagglutinins, and the hemoglobin receptor protein, which are important for the bacterium to colonize and proliferate in the gingival crevice and to invade the periodontium. These findings strongly indicate critical roles of Rgp and Kgp in the virulence of P. gingivalis.
AB - Porphyromonas gingivalis, one of the major causative agents of periodontal diseases, produces large amounts of arginine- and lysine-specific cysteine proteinases in cell-associated and secretory forms, which are now referred to as Arg-gingipain (Rgp) and Lysgingipain (Kgp), respectively. A number of studies have revealed that these proteinases are closely associated with the periodontopathogenesis of this bacterium: destruction of periodontal connective tissues, disruption of host defense mechanisms, and development and maintenance of inflammation in periodontal pockets. With respect to the physiology of the bacterium, Rgp and Kgp are indispensable for it to obtain nutrients from the environment, since it cannot utilize saccharides as carbon/energy sources for growth and totally depends on peptides and amino acids that are provided from environmental proteins by Rgp and Kgp. Furthermore, proteolytic activities of Rgp and Kgp contribute to processing/maturation of various cell-surface proteins of P. gingivalis, such as fimA fimbrilin (a subunit of major fimbriae), 75-kDa protein (a subunit of minor fimbriae), hemagglutinins, and the hemoglobin receptor protein, which are important for the bacterium to colonize and proliferate in the gingival crevice and to invade the periodontium. These findings strongly indicate critical roles of Rgp and Kgp in the virulence of P. gingivalis.
KW - Arg-gingipain
KW - Cysteine proteinases
KW - Lys-gingipain
KW - Periodontal diseases
KW - Porphyromonas gingivalis
UR - http://www.scopus.com/inward/record.url?scp=0033857548&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033857548&partnerID=8YFLogxK
U2 - 10.1093/oxfordjournals.jbchem.a022735
DO - 10.1093/oxfordjournals.jbchem.a022735
M3 - Review article
C2 - 10920248
AN - SCOPUS:0033857548
SN - 0021-924X
VL - 128
SP - 153
EP - 159
JO - Journal of Biochemistry
JF - Journal of Biochemistry
IS - 2
M1 - 128.2.153
ER -