Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Inactivation of the Porphyromonas gingivalis fimA gene blocks periodontal damage in gnotobiotic rats.

Journal of bacteriology - 1 Feb 1994

Malek R, Fisher J G, Caleca A, Stinson M, van Oss C J, Lee J Y, Cho M I, Genco R J, Evans R T, Dyer D W

Abstract excerpt

Fimbrial production by Porphyromonas gingivalis was inactivated by insertion-duplication mutagenesis, using the cloned gene for the P. gingivalis major fimbrial subunit protein, fimA. by several criteria, this insertion mutation rendered P. gingivalis unable to produce fimbrilin or an intact fimbrial structure. A nonfimbriated mutant, DPG3, hemagglutinated sheep erythrocytes normally and was unimpaired in the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to Blotting, Western

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genes, Bacterial

Share to Mutagenesis, Insertional

Share to Mutation

Share to Plasmids

Share to Rats, Sprague-Dawley

Source

Open in PubMed Open full text

Identifiers

PMID: 8106316
DOI: 10.1128/jb.176.4.1052-1059.1994
PMCID: PMC205156

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inactivation of the Porphyromonas gingivalis fimA gene blocks periodontal damage in gnotobiotic rats.PMID 8106316Read ↗

Construction and characterization of a fimA mutant of Porphyromonas gingivalis.Semantic proximity Read ↗

Isolation and characterization of transposon-induced mutants of Porphyromonas gingivalis deficient in fimbriation.Semantic proximity Read ↗

Characterization of biologically active cell surface components of a periodontal pathogen. The roles of major and minor fimbriae of Porphyromonas gingivalis.Semantic proximity Read ↗

Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains.Semantic proximity Read ↗

Role of fimbriae in Porphyromonas gingivalis invasion of gingival epithelial cells.Semantic proximity Read ↗

Genetic Manipulation of Porphyromonas gingivalisSemantic proximity Read ↗

A Porphyromonas gingivalis mutant defective in a putative glycosyltransferase exhibits defective biosynthesis of the polysaccharide portions of lipopolysaccharide, decreased gingipain activities, strong autoaggregation, and increased biofilm formation.Semantic proximity Read ↗

Arginine deiminase inhibits Porphyromonas gingivalis surface attachmentSemantic proximity Read ↗

Resistance of a Tn4351-generated polysaccharide mutant of Porphyromonas gingivalis to polymorphonuclear leukocyte killing.Semantic proximity Read ↗

Site-Directed and Random Mutagenesis in Porphyromonas gingivalis: Construction of Fimbriae-Related-Gene Mutant.Semantic proximity Read ↗

Pleiotropic pigmentation mutants of Porphyromonas gingivalis.Semantic proximity Read ↗

Fimbriae of Porphyromonas gingivalis induce opsonic antibodies that significantly enhance phagocytosis and killing by human polymorphonuclear leukocytes.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.