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

Human Gb3/CD77 synthase produces P1 glycotope-capped N-glycans, which mediate Shiga toxin 1 but not Shiga toxin 2 cell entry.

The Journal of biological chemistry - 1 Jan 2000

Szymczak-Kulus Katarzyna, Weidler Sascha, Bereznicka Anna, Mikolajczyk Krzysztof, Kaczmarek Radoslaw, Bednarz Bartosz, Zhang Tao, Urbaniak Anna, Olczak Mariusz, Park Enoch Y, Majorczyk Edyta, Kapczynska Katarzyna, Lukasiewicz Jolanta, Wuhrer Manfred, Unverzagt Carlo, Czerwinski Marcin

Abstract excerpt

The human Gb3/CD77 synthase, encoded by the A4GALT gene, is an unusually promiscuous glycosyltransferase. It synthesizes the Galα1→4Gal linkage on two different glycosphingolipids (GSLs), producing globotriaosylceramide (Gb3, CD77, Pk) and the P1 antigen. Gb3 is the major receptor for Shiga toxins (Stxs) produced by enterohemorrhagic Escherichia coli. A single amino acid substitution (p.Q211E) ramps up the...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosamine
Share to Galactose

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

Share to Galactosyltransferases

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Shiga Toxin 1

Share to Shiga Toxin 2

Share to Trihexosylceramides

Source

Open in PubMed Open full text

Identifiers

PMID: 33460651
DOI: 10.1016/j.jbc.2021.100299
PMCID: PMC7949097

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

Human Gb3/CD77 synthase produces P1 glycotope-capped N-glycans, which mediate Shiga toxin 1 but not Shiga toxin 2 cell entry.PMID 33460651Read ↗

<i>B4GALT5</i> -deficient CHO-Lec2 cells expressing human α1,4-galactosyltransferase: a glycoengineered cell model for studying Shiga toxin receptorsSemantic proximity Read ↗

Shiga Toxins: An Update on Host Factors and Biomedical ApplicationsSemantic proximity Read ↗

Rapid evolution of bacterial AB5 toxin B subunits independent of A subunits: sialic acid binding preferences correlate with host range and toxicitySemantic proximity Read ↗

Surface functionalization of small extracellular vesicles derived from Caco-2 and HEK293T cells in the neutralization of Shiga toxin 1 subunit BSemantic proximity Read ↗

A mutant Shiga-like toxin IIe bound to its receptor Gb(3): structure of a group II Shiga-like toxin with altered binding specificity.Semantic proximity Read ↗

Glycosyltransferases involved in type 1 chain and Lewis antigen biosynthesis exhibit glycan and core chain specificitySemantic proximity Read ↗

Evolutionary and functional connections between the typhoid toxins encoded by <i>S.</i> Typhi and <i>S. bongori</i>Semantic proximity Read ↗

Neutralization of Shiga Toxins Stx1, Stx2c, and Stx2e by Recombinant Bacteria Expressing Mimics of Globotriose and GlobotetraoseSemantic proximity Read ↗

Structural and Functional Characterization of Stx2k, a New Subtype of Shiga Toxin 2Semantic proximity Read ↗

The interplay between Siglecs and sialylated pathogensSemantic proximity Read ↗

Hypofucosylation promotes pertussis toxin binding to cell surface glycococonjugates and pertussis toxin-induced intracellular ERK signalingSemantic proximity Read ↗

New insights into the structure-function relationships and therapeutic applications of cholera-like enterotoxins.Semantic proximity Read ↗

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