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

Molecular Basis of the Interaction between Complement Receptor Type 2 (CR2/CD21) and Epstein-Barr Virus Glycoprotein gp350

12 Sept 2008

Abstract excerpt

The binding of the Epstein-Barr virus glycoprotein gp350 by complement receptor type 2 (CR2) is critical for viral attachment to B lymphocytes. We set out to test hypotheses regarding the molecular nature of this interaction by developing an enzyme-linked immunosorbent assay (ELISA) for the efficient analysis of the gp350-CR2 interaction by utilizing wild-type and mutant forms of recombinant gp350 and also of the...

Read the complete abstract on PubMed

Topics

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

Share to Complement system in diseases
Share to Immunodeficiency and Autoimmune Disorders
Share to Viral-associated cancers and disorders

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

Source

Identifiers

PMID: 18786993
DOI: 10.1128/jvi.01673-08

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 21 Oct 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

Molecular Basis of the Interaction between Complement Receptor Type 2 (CR2/CD21) and Epstein-Barr Virus Glycoprotein gp350PMID 18786993Read ↗

Isolating the Epstein-Barr Virus gp350/220 Binding Site on Complement Receptor Type 2 (CR2/CD21)Semantic proximity Read ↗

Structural basis of Epstein-Barr virus gp350 receptor recognition and neutralizationSemantic proximity Read ↗

Structural basis for complement receptor engagement and virus neutralization through Epstein-Barr virus gp350Semantic proximity Read ↗

Structural requirements for C3d,g/Epstein-Barr virus receptor (CR2/CD21) ligand binding, internalization, and viral infection.Semantic proximity Read ↗

Human complement receptor type 1/CD35 is an Epstein-Barr Virus receptor.Semantic proximity Read ↗

The crystal structure of human CD21: Implications for Epstein–Barr virus and C3d bindingSemantic proximity Read ↗

Deciphering Complement Receptor Type 1 Interactions with Recognition Proteins of the Lectin Complement PathwaySemantic proximity Read ↗

Identification of a Novel Neutralizing and Two Non-Neutralizing Epitopes on Epstein-Barr Virus gp350 ProteinSemantic proximity Read ↗

Factor VIII C1 domain spikes 2092-2093 and 2158-2159 comprise regions that modulate cofactor function and cellular uptake.Semantic proximity Read ↗

Characterization of Human Complement Receptor Type 2 (CR2/CD21) as a Receptor for IFN-α: A Potential Role in Systemic Lupus ErythematosusSemantic proximity Read ↗

Mutational Analyses of Epstein-Barr Virus Glycoprotein 42 Reveal Functional Domains Not Involved in Receptor Binding but Required for Membrane FusionSemantic proximity Read ↗

Cr2, a candidate gene in the murine Sle1c lupus susceptibility locus, encodes a dysfunctional protein.Semantic proximity Read ↗

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