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

High-resolution asymmetric structure of a Fab-virus complex reveals overlap with the receptor binding site.

Proceedings of the National Academy of Sciences of the United States of America - 8 Jun 2021

Goetschius Daniel J, Hartmann Samantha R, Organtini Lindsey J, Callaway Heather, Huang Kai, Bator Carol M, Ashley Robert E, Makhov Alexander M, Conway James F, Parrish Colin R, Hafenstein Susan L

Abstract excerpt

Canine parvovirus is an important pathogen causing severe diseases in dogs, including acute hemorrhagic enteritis, myocarditis, and cerebellar disease. Overlap on the surface of parvovirus capsids between the antigenic epitope and the receptor binding site has contributed to cross-species transmission, giving rise to closely related variants. It has been shown that Mab 14 strongly binds and neutralizes canine but...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Viral
Share to Antigens

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Capsid

Share to Cryoelectron Microscopy

Share to Epitopes

Share to Immunoglobulin Fab Fragments

Share to Parvovirus, Canine

Share to Protein Domains

Source

Open in PubMed Open full text

Identifiers

PMID: 34074770
DOI: 10.1073/pnas.2025452118
PMCID: PMC8201801

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

High-resolution asymmetric structure of a Fab-virus complex reveals overlap with the receptor binding site.PMID 34074770Read ↗

Transferrin receptor binds virus capsid with dynamic motionSemantic proximity Read ↗

Parvovirus Capsid-Antibody Complex Structures Reveal Conservation of Antigenic Epitopes Across the FamilySemantic proximity Read ↗

Mapping Antigenic Epitopes on the Human Bocavirus CapsidSemantic proximity Read ↗

Viral Capsid, Antibody, and Receptor Interactions: Experimental Analysis of the Antibody Escape Evolution of Canine Parvovirus.Semantic proximity Read ↗

Viral capsid, antibody, and receptor interactions: experimental analysis of the antibody escape evolution of canine parvovirusSemantic proximity Read ↗

Structural Insights into Human BocaparvovirusesSemantic proximity Read ↗

Parvovirus Capsid Structures Required for Infection: Mutations Controlling Receptor Recognition and Protease Cleavages.Semantic proximity Read ↗

Complex and Dynamic Interactions between Parvovirus Capsids, Transferrin Receptors, and Antibodies Control Cell Infection and Host Range.Semantic proximity Read ↗

Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structureSemantic proximity Read ↗

Structures of Echovirus 30 in complex with its receptors inform a rational prediction for enterovirus receptor usageSemantic proximity Read ↗

Adeno-associated virus (AAV) cell entry: structural insightsSemantic proximity Read ↗

Adeno-associated Virus Receptor-binding: Flexible Domains and Alternative Conformations through cryo-Electron Tomography of AAV2 and AAV5 complexesSemantic proximity Read ↗

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