Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
ARGININE IS A COMMON LIGAND FOR HEMAGGLUTINATION AND PROTEIN-BINDING BY ORGANISMS INHABITING MUCOSAL SURFACES
Autore:
EGGERT FM; CHAN ECS; KLITORINOS A; FLOWERDEW G;
Indirizzi:
UNIV ALBERTA,FAC DENT,DEPT STOMATOL EDMONTON AB T6G 2N8 CANADA MCGILL UNIV,FAC DENT,DEPT ORAL BIOL MONTREAL PQ H3A 2B4 CANADA UNIV ALBERTA,FAC MED,DEPT PUBL HLTH SCI EDMONTON AB CANADA
Titolo Testata:
Microbial ecology in health and disease
fascicolo: 6, volume: 8, anno: 1995,
pagine: 267 - 280
SICI:
0891-060X(1995)8:6<267:AIACLF>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRYPSIN-LIKE ACTIVITY; PORPHYROMONAS-GINGIVALIS; BACTEROIDES-GINGIVALIS; PUTATIVE PERIODONTOPATHOGENS; HEMAGGLUTINATION ACTIVITY; FUSOBACTERIUM-NUCLEATUM; PERIODONTAL-DISEASE; HUMAN-ERYTHROCYTES; ORAL STRAINS; ADHERENCE;
Keywords:
PORPHYROMONAS GINGIVALIS; TREPONEMA DENTICOLA; T-VINCENTII; T-SOCRANSKII; HEMAGGLUTINATION; PROTEIN BINDING; ARGININE; LYSINE; GUANIDINIUM; ORAL MUCOSA; ADHERENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
F.M. Eggert et al., "ARGININE IS A COMMON LIGAND FOR HEMAGGLUTINATION AND PROTEIN-BINDING BY ORGANISMS INHABITING MUCOSAL SURFACES", Microbial ecology in health and disease, 8(6), 1995, pp. 267-280

Abstract

Treponema denticola, T. vincentii and T. socranskii can be added to the diverse group of oral organisms which haemagglutinate via surface receptors that bind proteins and peptides. Model peptides and selectivechemical modification of arginyl or lysyl residues of protein ligandsshowed that for both Polphyromonas gingivalis and oral Treponema, binding involves predominantly arginyl and some lysyl residues. We have previously identified a relationship between protein binding, proteolytic activity and haemagglutination in P. gingivalis and were able to extend this finding to oral Treponema. Oral spirochaetes have both trypsin- and chymotrypsin-like proteases and peptidases and their haemagglutinins are blocked by both trypsin and chymotrypsin inhibitors. The narrow specificity of haemagglutination by these protein- and peptide-binding organisms allows a variety of dissimilar proteins in the oral environment to block haemagglutination. Possession of arginyl-directed haemagglutinins by both the non-motile P. gingivalis and the motile Treponema indicates that adherence to oral surfaces must involve additional mechanisms beyond those demonstrated by in vitro clumping of erythrocytes. The bulky structure and intense charge of the guanidinium group of arginine appear to make this amino acid residue an 'ideal' ligandin the mucosal environment. Binding of proteins via the guanidinium group of arginine is a widely-occurring adaptation among different species of oral microbes. Agents such as chlorhexidine that also possess guanidinium groups would interfere with the central role of arginine asa ligand involved in a variety of binding reactions exhibited by bacteria inhabiting mucosal surfaces.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 19:31:10