Search Antibody Database

Found 2 matching records:

Displaying record number 477

Download this epitope record as JSON.

MAb ID	SP.BAL114
HXB2 Location	gp160(308-317) DNA(7146..7175)	gp160 Epitope Map
Author Location	gp120( BAL)
Epitope	SIHIGPGRAF	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse(IgG2aκ)
Patient
Immunogen
Keywords

Notes

Showing 2 of 2 notes.

• SP.BAL114: Similarity level of the SP.BAL114 binding site pentapeptide IHIGP to the host proteome was low, with the low-similarity 5-mer occurring in the host proteome 0 times, indicating that this peptide can be used to elicit Abs for active/passive immunotherapy with low risk of cross-reaction with the host proteome. Kanduc2008
• Authors suggest that during in vivo immunoselection of escape virus, the V3 domain gains increasing resemblance to that of lab strains. Arendrup1995

References

Showing 2 of 2 references.

Arendrup1995 M. Arendrup, L. Akerblom, P. M. Heegaard, J. O. Nielsen, and J. E. Hansen. The HIV-1 V3 domain on field isolates: participation in generation of escape virus in vivo and accessibility to neutralizing antibodies. Arch. Virol., 140:655-670, 1995. The anti-V3 Ab titre in patient serum was generally low against autologous virus isolated later than the serum sample, in contrast to a higher titre against peptides corresponding to virus isolated earlier than the serum sample. The authors conclude that the V3 domain is subject to immunoselection in vivo, and that V3 on early field virus is less accessible to NAbs than the V3 loop on laboratory strains. PubMed ID: 7794110. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.

Displaying record number 2475

Download this epitope record as JSON.

MAb ID	0.5γ (1C10)
HXB2 Location	gp160(308-317)	gp160 Epitope Map
Author Location	gp120
Epitope	SIHIGPGRAF	Epitope Alignment
Subtype	B
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	P (tier 2)  View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human(IgG1κ)
Patient	KTS376
Immunogen	HIV-1 infection
Country	Japan
Keywords	ADCC, antibody binding site, antibody generation, binding affinity, drug resistance, mimics, neutralization

Notes

Showing 3 of 3 notes.

• 0.5γ: Cells lines containing HIV from patient KK were passaged in the presence of ceniciviroc (CVC) to derive CVC-resistant strains. These strains were sensitive to antibodies, including 0.5γ, 4E9C, and 49G2. Resistance to 0.5γ and 4E9C was caused by novel substitutions R315K, G324R, and E381K. These loci occur near substitutions conferring resistance to CVC, and these changes are associated with a reversion to a CVC-sensitive phenotype. These results suggest that CVC and NAbs may restrict the emergence of variants resistant to each other. Kuwata2016 (drug resistance, neutralization)
• 0.5γ(1C10): B-cell clones derived from a long-term non-progressive patient were selected for MAbs reactive to gp120. These MAbs bound to several complementary regions of gp120 and synergistically neutralized a wide range of HIV subtypes. This could be an alternative method to induction of bNAbs. 0.5γ had ADCC activity. Median neutralization potency against 9/11 laboratory and primary strains was high, between 0.05-10 µl; and spanning high-medium-low against 10 subtype B of a standard panel of 27 HIV-1; potency against autologous virus was low. MAb 0.5gamma had significant ADCC activity against cells infected with 3 of 3 lab strains and 3 of 5 T/F strains tested. RamirezValdez2015 (ADCC, antibody binding site, neutralization, binding affinity)
• 0.5γ: MAbs were established from a patient with long-term nonprogressive illness. B cells from the patient’s PBMC were transformed by Epstein-Barr virus, followed by cloning. Pretreatment by the small NBD-556 CD4-mimicking compound remarkably increased binding of 0.5γ to JR-FL Env, indicating enhancement of 0.5γ epitope accessibility by NBD-556. Yoshimura2010 (ADCC, antibody generation, mimics, binding affinity)

References

Showing 3 of 3 references.

Isolation Paper
Yoshimura2010 Kazuhisa Yoshimura, Shigeyoshi Harada, Junji Shibata, Makiko Hatada, Yuko Yamada, Chihiro Ochiai, Hirokazu Tamamura, and Shuzo Matsushita. Enhanced Exposure of Human Immunodeficiency Virus Type 1 Primary Isolate Neutralization Epitopes through Binding of CD4 Mimetic Compounds. J. Virol., 84(15):7558-7568, Aug 2010. PubMed ID: 20504942. Show all entries for this paper.

Kuwata2016 Takeo Kuwata, Ikumi Enomoto, Masanori Baba, and Shuzo Matsushita. Incompatible Natures of the HIV-1 Envelope in Resistance to the CCR5 Antagonist Cenicriviroc and to Neutralizing Antibodies. Antimicrob. Agents Chemother., 60(1):437-450, 2 Nov 2015. PubMed ID: 26525792. Show all entries for this paper.

RamirezValdez2015 Kristel Paola Ramirez Valdez, Takeo Kuwata, Yasuhiro Maruta, Kazuki Tanaka, Muntasir Alam, Kazuhisa Yoshimura, and Shuzo Matsushita. Complementary and Synergistic Activities of Anti-V3, CD4bs and CD4i Antibodies Derived from a Single Individual Can Cover a Wide Range of HIV-1 Strains. Virology, 475:187-203, 15 Jan 2015. PubMed ID: 25486586. Show all entries for this paper.