Back to search

Article

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

2022-04-22

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, proteolyti...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
f125bb57-9dfc-58b4-9d1b-505140f4d6ef
DOI
10.21203/rs.3.rs-1534769/v1
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Engineering of HIV-1 neutralizing antibody CAP256V2LS for manufacturability and improved half lifeDOI 10.21203/rs.3.rs-1534769/v1
Engineering of HIV-1 neutralizing antibody CAP256V2LS for manufacturability and improved half lifeSemantic proximity
Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop.Semantic proximity
New Member of the V1V2-Directed CAP256-VRC26 Lineage That Shows Increased Breadth and Exceptional PotencySemantic proximity
Improved pharmacokinetics of HIV-neutralizing VRC01-class antibodies achieved by reduction of net positive charge on variable domainSemantic proximity
Structure-guided design of native-like HIV Env Single Chain Trimers for enhanced stability, immunogenicity, and versatile vaccine deliverySemantic proximity
Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding SiteSemantic proximity
A Randomised Clinical Trial of the Safety and Pharmacokinetics of VRC07-523LS Administered via Different Routes and Doses (HVTN 127/HPTN 087)Semantic proximity
V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC ActivitySemantic proximity
Dependence on a variable residue limits the breadth of an HIV MPER neutralizing antibody, despite convergent evolution with broadly neutralizing antibodiesSemantic proximity
IgG3 enhances neutralization potency and Fc effector function of an HIV V2-specific broadly neutralizing antibodySemantic proximity
Optimization of the Solubility of HIV-1-Neutralizing Antibody 10E8 through Somatic Variation and Structure-Based DesignSemantic proximity
Translating Innovation to Clinic: End-to-End Bioprocess Development and cGMP Manufacturing of N332-GT5 HIV Vaccine Candidate for First-in-Human Trials HVTN144Semantic proximity
Select a neighboring publication to make it the new centre.