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MAb ID	m44
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type	C-HR
Neutralizing
Species (Isotype)	human
Patient
Immunogen	HIV-1 infection
Keywords	ADCC, antibody binding site, antibody generation, antibody sequence, binding affinity, neutralization, variant cross-reactivity

Notes

Showing 3 of 3 notes.

m44: Isolation of human mAb, E10, from an HIV-1-infected patient sample by single B cell sorting and single cell PCR has been reported. E10 showed binding to gp140 trimer and linear peptides derived from gp41 membrane proximal external region (MPER). E Mab E10 showed less reactivity with human self-antigens e.g., phospholipids, including CL, Ro (SSA), centromere B, and histones in comparison with m44 when measured by AtheNA antinuclear autoantibody assay. m44 didn't bind to CL Yang2018 (ADCC)
m44: Ab gene divergence analyses found that m44 Ab was significantly more divergent from the closest germline Abs than were hmAbs against other viruses. Germline-like m44 was constructed in a scFv format. It was shown that, unlike b12, 2G12 and 2F5, germline-like m44 bound to recombinant gp140, however with lower affinity than the corresponding mature m44 MAb. Xiao2009 (binding affinity, antibody sequence)
m44: The highly neutralizing Ab m44 was isolated by phage library panning, derived from three HIV-1 infected long term nonprogressors with sera with broadest and most potent neutralization. The phage library was panned with uncleaved Env ectodomains and the derived m44 MAb was shown to neutralize primary isolates from different clades with potency significantly higher than that of 4E10 or Z13. m44 neutralized clade C SHIV more potently than 2F5 and b12. The neutralization potency of m44 was significantly higher in PBMC than in TZM-bl cell-line based assay. Site-directed alanine-scanning mutagenesis revealed that the epitope for m44 is conserved, conformational, and is located at the C-HR and a stretch of residues at the C-terminal portion of the loop. m44 did not bind to human self-antigens. Zhang2008 (antibody binding site, antibody generation, neutralization, variant cross-reactivity)

References

Showing 3 of 3 references.

Isolation Paper
Zhang2008 Mei-Yun Zhang, Bang K. Vu, Anil Choudhary, Hong Lu, Michael Humbert, Helena Ong, Munir Alam, Ruth M. Ruprecht, Gerald Quinnan, Shibo Jiang, David C. Montefiori, John R. Mascola, Christopher C. Broder, Barton F. Haynes, and Dimiter S. Dimitrov. Cross-Reactive Human Immunodeficiency Virus Type 1-Neutralizing Human Monoclonal Antibody That Recognizes a Novel Conformational Epitope on gp41 and Lacks Reactivity against Self-Antigens. J. Virol., 82(14):6869-6879, Jul 2008. PubMed ID: 18480433. Show all entries for this paper.

Xiao2009 Xiaodong Xiao, Weizao Chen, Yang Feng, Zhongyu Zhu, Ponraj Prabakaran, Yanping Wang, Mei-Yun Zhang, Nancy S. Longo, and Dimiter S. Dimitrov. Germline-Like Predecessors of Broadly Neutralizing Antibodies Lack Measurable Binding to HIV-1 Envelope Glycoproteins: Implications for Evasion of Immune Responses and Design of Vaccine Immunogens. Biochem. Biophys. Res. Commun., 390(3):404-409, 18 Dec 2009. PubMed ID: 19748484. Show all entries for this paper.

Yang2018 Zheng Yang, Xi Liu, Zehua Sun, Jingjing Li, Weiguo Tan, Weiye Yu, and Meiyun Zhang. Identification of a HIV gp41-Specific Human Monoclonal Antibody with Potent Antibody-Dependent Cellular Cytotoxicity. Front. Immunol., 9:2613, 2018. PubMed ID: 30519238. Show all entries for this paper.