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Displaying record number 1407

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MAb ID	SAR1
HXB2 Location	gp160(738-744) DNA(8436..8456)	gp160 Epitope Map
Author Location	gp41(735-752 IIIB)
Epitope	`GERDRDR`	Epitope Alignment
Subtype	B
Ab Type	C-term
Neutralizing
Species (Isotype)	mouse(IgG2aκ)
Patient
Immunogen	vaccine
Keywords	antibody binding site, binding affinity, review

Vaccine Details

Vaccine type	Cowpea mosaic virus
Vaccine component	gp41

Notes

Showing 4 of 4 notes.

SAR1: The two distinct and conflicting models of C-terminal tail (CTT) topology for HIV-1 gp41 were tested by characterizing the accessibility of KE (Kennedy epitope) sequences of gp41 to Ab binding on the surface of Env-expressing cells and intact mature virions. SAR1 has accessibility to KE sequence in intact cells expressing Env ( HIV-1 89.6 Env): WT, VSV-G-KE (VSG-G tag substituted in KE) and VSV-G-LLP2 (VSG-G tag substituted in LLP2) . SAR1 fails to bind to KE in the context of intact virions. Steckbeck2010 (binding affinity)
SAR1: Unlike the MPER MAbs tested, SAR1 did not show any Env-independent virus capture in the conventional or in the modified version of the virus capture assay. Leaman2010
SAR1: This paper confirms the post-attachment neutralization (PAN) activity of this gp41 C-terminal tail-specific Ab -- cell fusion between infected and uninfected cells is inhibited and is temperature dependent. This MAb does not neutralize free virus, and due to PAN activity, is considered to bind an epitope on the external surface of the membrane. The SAR1 epitope is exposed optimally after infected and non-infected cells have attached, prior to fusion. sCD4 binding does not enhance binding of SAR1. MAbs to adjacent epitopes do not have PAN activity. Heap2005a (antibody binding site)
SAR1: This ERDRD-specific MAb recognizes an externalized loop of the gp41 C-terminal domain, and can reduce the yield of infectious progeny and inhibit fusion post-attachment, but not neutralize free virus. Dimmock2005 (review)

References

Showing 4 of 4 references.

Dimmock2005 Nigel J. Dimmock. The Complex Antigenicity of a Small External Region of the C-Terminal Tail of the HIV-1 gp41 Envelope Protein: A Lesson in Epitope Analysis. Rev. Med. Virol., 15(6):365-381, Nov-Dec 2005. PubMed ID: 16106492. Show all entries for this paper.

Heap2005a Caroline J. Heap, Steven A. Reading, and Nigel J. Dimmock. An Antibody Specific for the C-Terminal Tail of the gp41 Transmembrane Protein of Human Immunodeficiency Virus Type 1 Mediates Post-Attachment Neutralization, Probably Through Inhibition of Virus-Cell Fusion. J. Gen. Virol., 86(5):1499-1507, May 2005. PubMed ID: 15831963. Show all entries for this paper.

Leaman2010 Daniel P. Leaman, Heather Kinkead, and Michael B. Zwick. In-Solution Virus Capture Assay Helps Deconstruct Heterogeneous Antibody Recognition of Human Immunodeficiency Virus Type 1. J. Virol., 84(7):3382-3395, Apr 2010. PubMed ID: 20089658. Show all entries for this paper.

Steckbeck2010 Jonathan D. Steckbeck, Chengqun Sun, Timothy J. Sturgeon, and Ronald C. Montelaro. Topology of the C-Terminal Tail of HIV-1 gp41: Differential Exposure of the Kennedy Epitope on Cell and Viral Membranes. PLoS One, 5(12):e15261, 2010. PubMed ID: 21151874. Show all entries for this paper.