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Displaying record number 1431

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MAb ID	LA21
HXB2 Location	Env	Env Epitope Map
Author Location
Epitope
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing
Species (Isotype)	human
Patient	AC-05
Immunogen
Keywords	antibody binding site, binding affinity, glycosylation, neutralization, structure, variant cross-reactivity

Notes

Showing 5 of 5 notes.

LA21: This paper reported the nature of junk Env glycan that undermine the development of Ab responses against gp120/gp41 trimers and evaluated enzyme digestion as a way to remove aberrant Env to produce "trimer VLPs". LA21 was used in the anti-gp120 cocktail in the western blot experiment to prove that enzymes removed junk Env from VLPs and inactivated virus.. Crooks2011 (glycosylation)
LA21: Antigenic properties of undigested VLPs and endo H-digested WT trimer VLPs were compared. Binding of LA21 to WT VLPs is consistent with the recognition of nonfunctional Env. LA21 did not neutralize trimer VLPs. BN-PAGE shifts using digested E168K + N189A WT trimer VLPs exhibited prominence compared to WT VLPs. Tong2012 (neutralization, binding affinity)
LA21: LA21 neutralized two of the 15 subtype B isolates tested. Binding affinity of MAb LA21 to gp120 was strongly reduced upon substitutions of His308, or Pro313 (250-fold), to Ala. The dependence on Pro313 suggests that a precise conformation of the V3 β hairpin turn may be critical for binding of LA21. Thus, LA21 may need to interact with V3 from an angle, which does not permit access to V3 on many different primary viruses. LA21 inability to neutralize 6 of the 15 viruses tested could not be explained by substitution of important contact residues. The fine specificity of LA21 was mapped onto V3 in the structural context of gp120. This showed that the residues important for LA21 binding form a somewhat disjointed pattern, and that LA21 likely also contacts neighboring residues. Pantophlet2008 (antibody binding site, neutralization, variant cross-reactivity, binding affinity, structure)
LA21: This Ab was shown not to react with clade C gp140 (97CN54). Sheppard2007a (variant cross-reactivity)
LA21: Of 35 Env-specific MAbs tested, only 2F5, 4E10, IgG1b12, and two CD4BS adjacent MAbs (A32 and 1.4G) and gp41 MAbs (2.2B and KU32) binding patterns suggesting polyspecific autoreactivity, and similar reactivities may be difficult to induce with vaccines because of elimination of such autoreactivity. LA21 has no indication of polyspecific autoreactivity. Haynes2005 (antibody binding site)

References

Showing 5 of 5 references.

Haynes2005 Barton F. Haynes, Judith Fleming, E. William St. Clair, Herman Katinger, Gabriela Stiegler, Renate Kunert, James Robinson, Richard M. Scearce, Kelly Plonk, Herman F. Staats, Thomas L. Ortel, Hua-Xin Liao, and S. Munir Alam. Cardiolipin Polyspecific Autoreactivity in Two Broadly Neutralizing HIV-1 Antibodies. Science, 308(5730):1906-1908, 24 Jun 2005. Comment in Science 2005 Jun 24;308(5730):1878-9. PubMed ID: 15860590. Show all entries for this paper.

Sheppard2007a Neil C. Sheppard, Sarah L. Davies, Simon A. Jeffs, Sueli M. Vieira, and Quentin J. Sattentau. Production and Characterization of High-Affinity Human Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Envelope Glycoproteins in a Mouse Model Expressing Human Immunoglobulins. Clin. Vaccine Immunol., 14(2):157-167, Feb 2007. PubMed ID: 17167037. Show all entries for this paper.

Pantophlet2008 Ralph Pantophlet, Terri Wrin, Lisa A. Cavacini, James E. Robinson, and Dennis R. Burton. Neutralizing Activity of Antibodies to the V3 Loop Region of HIV-1 gp120 Relative to Their Epitope Fine Specificity. Virology, 381(2):251-260, 25 Nov 2008. PubMed ID: 18822440. Show all entries for this paper.

Tong2012 Tommy Tong, Ema T. Crooks, Keiko Osawa, and James M. Binley. HIV-1 Virus-Like Particles Bearing Pure Env Trimers Expose Neutralizing Epitopes but Occlude Nonneutralizing Epitopes. J. Virol., 86(7):3574-3587, Apr 2012. PubMed ID: 22301141. Show all entries for this paper.

Crooks2011 Ema T. Crooks, Tommy Tong, Keiko Osawa, and James M. Binley. Enzyme Digests Eliminate Nonfunctional Env from HIV-1 Particle Surfaces, Leaving Native Env Trimers Intact and Viral Infectivity Unaffected. J. Virol., 85(12):5825-5839, Jun 2011. PubMed ID: 21471242. Show all entries for this paper.