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

Cloning of a locus involved in Streptococcus mutans intracellular polysaccharide accumulation and virulence testing of an intracellular polysaccharide-deficient mutant.

Infection and immunity - 1 Aug 1992

Harris G S, Michalek S M, Curtiss R

Abstract excerpt

The streptococcal transposon Tn916 (Tcr) was used to isolate mutants of Streptococcus mutans altered in glycogen accumulation to investigate whether glycogenlike intracellular polysaccharides (IPS) play an important role in S. mutans-induced caries formation. S. mutans UA130 (serotype c) was transformed with the Escherichia coli plasmid pAM620 (Tn916), and the resultant transposon libraries were screened for...

Read the complete abstract on PubMed

Topics

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

Share to Chromosome Mapping
Share to Cloning, Molecular

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

Share to DNA Transposable Elements

Share to Genetic Complementation Test

Share to Mutation

Share to Rats, Inbred F344

Share to Virulence

Source

Open in PubMed Open full text

Identifiers

PMID: 1322367
DOI: 10.1128/iai.60.8.3175-3185.1992
PMCID: PMC257299

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

Cloning of a locus involved in Streptococcus mutans intracellular polysaccharide accumulation and virulence testing of an intracellular polysaccharide-deficient mutant.PMID 1322367Read ↗

A Streptococcus mutans mutant that synthesizes elevated levels of intracellular polysaccharide is hypercariogenic in vivoSemantic proximity Read ↗

Ribosomal-processing cysteine protease homolog modulates Streptococcus mutans glucan production and interkingdom interactions.Semantic proximity Read ↗

Inactivation ofStreptococcus mutansgeneslytSTanddltADimpairs its pathogenicityin vivoSemantic proximity Read ↗

Alterations in the cellular envelope of spontaneous IIIManL-defective mutants of Streptococcus salivarius.Semantic proximity Read ↗

Structural and Molecular Basis of the Role of Starch and Sucrose in <i>Streptococcus mutans</i> Biofilm DevelopmentSemantic proximity Read ↗

Regulation of water‐soluble glucan synthesis by the Streptococcus mutans dexA gene effects biofilm aggregation and cariogenic pathogenicitySemantic proximity Read ↗

Mutants of Streptococcus gordonii Challis over-producing glucosyltransferase.Semantic proximity Read ↗

Involvement of an inducible fructose phosphotransferase operon in Streptococcus gordonii biofilm formation.Semantic proximity Read ↗

Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties.Semantic proximity Read ↗

Deficiency of RgpG Causes Major Defects in Cell Division and Biofilm Formation, and Deficiency of LytR-CpsA-Psr Family Proteins Leads to Accumulation of Cell Wall Antigens in Culture Medium by Streptococcus mutansSemantic proximity Read ↗

Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis: biosynthesis and impact on the persistence in mice.Semantic proximity Read ↗

Comprehensive mutational analysis of sucrose-metabolizing pathways in Streptococcus mutans reveals novel roles for the sucrose phosphotransferase system permease.Semantic proximity Read ↗

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