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 and characterization of sialidases with 2-6' and 2-3' sialyl lactose specificity from Pasteurella multocida.

Journal of bacteriology - 1 Dec 2000

Mizan S, Henk A, Stallings A, Maier M, Lee M D

Abstract excerpt

Pasteurella multocida is a mucosal pathogen that colonizes the respiratory system of susceptible hosts. Most isolates of P. multocida produce sialidase activity, which may contribute to colonization of the respiratory tract or the production of lesions in an active infection. We have cloned and sequenced a sialidase gene, nanH, from a fowl cholera isolate of P. multocida. Sequence analysis of NanH revealed that...

Read the complete abstract on PubMed

Topics

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

Share to Hydrogen-Ion Concentration
Share to Lactose
Share to N-Acetylneuraminic Acid

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

Share to Neuraminidase

Share to Pasteurella multocida

Share to Sequence Alignment

Share to Sialic Acids

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 11092845
DOI: 10.1128/JB.182.24.6874-6883.2000
PMCID: PMC94810

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 and characterization of sialidases with 2-6' and 2-3' sialyl lactose specificity from Pasteurella multocida.PMID 11092845Read ↗

Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity.Semantic proximity Read ↗

The group B streptococcal sialic acid O-acetyltransferase is encoded by neuD, a conserved component of bacterial sialic acid biosynthetic gene clusters.Semantic proximity Read ↗

The Sialidases of Clostridium perfringens type D strain CN3718 differ in their properties and sensitivities to inhibitors.Semantic proximity Read ↗

A semi-multifunctional sialyltransferase from Bibersteinia trehalosi and its comparison to the Pasteurella multocida ST1 mutants.Semantic proximity Read ↗

Decreasing the sialidase activity of multifunctional Pasteurella multocida α2-3-sialyltransferase 1 (PmST1) by site-directed mutagenesis.Semantic proximity Read ↗

Sialic acid metabolism's dual function in Haemophilus influenzae.Semantic proximity Read ↗

A sialyltransferase mutant with decreased donor hydrolysis and reduced sialidase activities for directly sialylating LewisX.Semantic proximity Read ↗

Role of <i>Tannerella forsythia</i> NanH Sialidase in Epithelial Cell AttachmentSemantic proximity Read ↗

CpsK of Streptococcus agalactiae exhibits alpha2,3-sialyltransferase activity in Haemophilus ducreyi.Semantic proximity Read ↗

Characterization of Histophilus somni sialic acid uptake mutant (ΔnanP-ΔnanU) using a mouse septicemia and mortality model.Semantic proximity Read ↗

Identification of an N-acetylneuraminic acid-presenting bacteria isolated from a healthy human microbiomeSemantic proximity Read ↗

Sialic Acid Transport Contributes to Pneumococcal ColonizationSemantic proximity Read ↗

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