Antibodies to HIV integrase catalyze site-specific degradation of their antigen

Autor: Valentina N. Buneva, Olga D. Zakharova, Marie-Line Andreola, Valeriy A. Rasskazov, Georgy A. Nevinsky, Elena S. Odintsova, Vincent Parissi, Pavel S. Dmitrenok, Christina Calmels, Svetlana V. Baranova
Přispěvatelé: Microbiologie cellulaire et moléculaire et pathogénicité (MCMP), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2011
Předmět:
Male
HIV Antigens
HIV Infections
HIV Integrase
HIV Antibodies
Substrate Specificity
Immunology and Allergy
MESH: Immunoglobulin G
0303 health sciences
Oligopeptide
Chymotrypsin
biology
030302 biochemistry & molecular biology
Proteolytic enzymes
General Medicine
MESH: HIV Infections
Trypsin
MESH: Immunoglobulin M
3. Good health
Integrase
[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology
Biochemistry
MESH: Young Adult
Female
MESH: Biocatalysis
medicine.drug
Adult
Proteases
Adolescent
Immunology
03 medical and health sciences
Young Adult
Affinity chromatography
medicine
Humans
030304 developmental biology
MESH: Adolescent
MESH: Humans
MESH: HIV Antibodies
MESH: Adult
Proteinase K
Molecular biology
MESH: Male
Immunoglobulin M
Immunoglobulin G
biology.protein
Biocatalysis
MESH: Substrate Specificity
MESH: HIV Integrase
MESH: Female
MESH: HIV Antigens
Zdroj: International Immunology
International Immunology, Oxford University Press (OUP), 2011, 23 (10), pp.601-12. ⟨10.1093/intimm/dxr065⟩
ISSN: 1460-2377
0953-8178
DOI: 10.1093/intimm/dxr065⟩
Popis: International audience; HIV-1 integrase (IN) catalyzes integration of a DNA copy of the viral genome into the host genome. In contrast to canonical proteases (trypsin, chymotrypsin and proteinase K), IgGs and IgMs isolated from HIV-infected patients by affinity chromatography on immobilized IN specifically hydrolyzed only IN but not many other tested intact globular proteins. The sites of IN cleavage determined by MALDI mass spectrometry were localized mainly within seven known immunodominant regions of IN. Thin layer chromatography analysis has shown that the abzymes (Abzs) could also cleave 17 to 22-mer oligopeptides (OPs) corresponding to the immunodominant regions of IN sequence with a much higher rate than non-specific long peptides or three- and tetrapeptides of various sequence. Therefore, a prolonged incubation of IN with AIDS IgGs and IgMs having high catalytic activity usually produces many OPs of different length. Since anti-IN IgGs and IgMs can efficiently hydrolyze IN, a positive role of the Abzs in counteracting the infection is possible.
Databáze: OpenAIRE