Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Functional characteristics of antibodies induced by Arg-gingipain (HRgpA) and Lys-gingipain (Kgp) from Porphyromonas gingivalis
Autore:
Nakagawa, T; Sims, T; Fan, Q; Potempa, J; Travis, J; Houston, L; Page, RC;
Indirizzi:
Univ Washington, Sch Dent, Dept Periodont, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ept Periodont, Seattle, WA 98195 USA Tokyo Dent Coll, Chiba, Japan Tokyo Dent Coll Chiba JapanTokyo Dent Coll, Chiba, Japan Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Biochem & Mol Biol, Athens, GA 30602 USA Jagiellonian Univ, Dept Microbiol & Immunol, Krakow, Poland Jagiellonian Univ Krakow Poland ept Microbiol & Immunol, Krakow, Poland
Titolo Testata:
ORAL MICROBIOLOGY AND IMMUNOLOGY
fascicolo: 4, volume: 16, anno: 2001,
pagine: 202 - 211
SICI:
0902-0055(200108)16:4<202:FCOAIB>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAPIDLY PROGRESSIVE PERIODONTITIS; LIGATURE-INDUCED PERIODONTITIS; BACTEROIDES-GINGIVALIS; PREVOTELLA-INTERMEDIA; CYSTEINE PROTEINASES; ACTINOBACILLUS-ACTINOMYCETEMCOMITANS; MACACA-FASCICULARIS; CAPSULAR SEROTYPES; CYNOMOLGUS MONKEY; MOLECULAR-CLONING;
Keywords:
Porphyromonas gingivalis; ELISA; antibodies; opsonization; polymorphonuclear leukocytes;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Page, RC Univ Washington, Sch Dent, Dept Periodont, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 dont, Seattle, WA 98195 USA
Citazione:
T. Nakagawa et al., "Functional characteristics of antibodies induced by Arg-gingipain (HRgpA) and Lys-gingipain (Kgp) from Porphyromonas gingivalis", ORAL MICROB, 16(4), 2001, pp. 202-211

Abstract

Arginine-specific gingipain (HRgpA) and lysine-specific gingipain (Kgp), enzymes produced by Porphyromonas gingivalis, may be candidates for an anti-P. gingivalis vaccine. The purpose of our study was to determine whether HRgpA and Kgp have opsonic target sites and whether these sites are availableand accessible on intact P. gingivalis cells. Rabbits were used to generate polyclonal antibodies to both proteins. Animals were immunized and immunoglobulin G (IgG) fractions were isolated from preimmune and immune sera. Functional Characteristics of the antibodies were assessed by determining antibody titers by enzyme-linked immunosorbent assay (ELISA), generating Western immunoblots, and measuring antibody enhancement of P. gingivalis opsonization, phagocytosis and killing by polymorphonuclear leukocytes (PMN) of intact cells of strains of P. gingivalis representative of the four serotypes. Strains studied included 33277 (serotype A), A7A1-28 (serotype B), W50 (serotype C) and 381 (serotype D). Both HRgpA and Kgp induced high titers of IgG antibody. Anti-HRgpA and anti-Kgp bound to both HRgpA and Kgp demonstrating a large proportion of shared antigenic epitopes. The two antibodies bound equally well to all four P. gingivalis serotypes with titers ranging from 77 to 205 ELISA units when compared to preimmune IgG set at 1 ELISA unit. The immunoblot patterns of binding of the two antibodies to HRgpA and Kgpand to sonicates of the four P. gingivalis serotypes were virtually identical. Both antibodies detected components in HRgpA at 27, 35 and 45 kDa and in Kgp at 27, 32, 35, 40 and 55 kDa. The antibodies also detected components at or near these same positions in addition to multiple high molecular mass components in the cell sonicates of P. gingivalis. Both proteins inducedantibodies that significantly enhanced opsonization as assessed by chemiluminescence, with values ranging from 130 mV to 375 mV for anti-HRgpA IgG and from 240 mV to 375 mV for anti-Kgp IgG. Both antibodies significantly enhanced PMN-mediated bacterial killing of the four P. gingivalis serotypes, although the percentage of killing varied among the serotypes (24-81% for anti-HRgpA and 37-89% for anti-Kgp). Thus, both HRgpA and Kgp express opsonictarget sites and induce high titers of antibodies that opsonize and enhance killing of all four serotypes of P. gingivalis. These two proteins appearto be potential candidate antigens for an anti-P. gingivalis vaccine.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 13:19:19