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

Engineering of HIV-1 neutralizing antibody CAP256V2LS for manufacturability and improved half life

25 Oct 2022

Abstract excerpt

The broadly neutralizing antibody (bNAb) CAP256-VRC26.25 has exceptional potency against HIV-1 and has been considered for clinical use. During the characterization and production of this bNAb, we observed several unusual features. First, the antibody appeared to adhere to pipette tips, requiring tips to be changed during serial dilution to accurately measure potency. Second, during production scale-up,...

Read the complete abstract on PubMed

Topics

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

Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36284200
DOI: 10.1038/s41598-022-22435-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineering of HIV-1 neutralizing antibody CAP256V2LS for manufacturability and improved half lifePMID 36284200Read ↗

Engineering of HIV-1 neutralizing antibody CAP256V2LS for manufacturability and improved half lifeSemantic proximity Read ↗

Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop.Semantic proximity Read ↗

New Member of the V1V2-Directed CAP256-VRC26 Lineage That Shows Increased Breadth and Exceptional PotencySemantic proximity Read ↗

Improved pharmacokinetics of HIV-neutralizing VRC01-class antibodies achieved by reduction of net positive charge on variable domainSemantic proximity Read ↗

Structure-guided design of native-like HIV Env Single Chain Trimers for enhanced stability, immunogenicity, and versatile vaccine deliverySemantic proximity Read ↗

Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding SiteSemantic proximity Read ↗

A Randomised Clinical Trial of the Safety and Pharmacokinetics of VRC07-523LS Administered via Different Routes and Doses (HVTN 127/HPTN 087)Semantic proximity Read ↗

Viral variants that initiate and drive maturation of V1V2-directed HIV-1 broadly neutralizing antibodies.Semantic proximity Read ↗

V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC ActivitySemantic proximity Read ↗

Dependence on a variable residue limits the breadth of an HIV MPER neutralizing antibody, despite convergent evolution with broadly neutralizing antibodiesSemantic proximity Read ↗

Enhanced Potency of a Broadly Neutralizing HIV-1 Antibody <i>In Vitro</i> Improves Protection against Lentiviral Infection <i>In Vivo</i>Semantic proximity Read ↗

Optimization of the Solubility of HIV-1-Neutralizing Antibody 10E8 through Somatic Variation and Structure-Based DesignSemantic proximity Read ↗

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