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Titolo:
ASSEMBLY AND ANTIGENICITY OF THE NEISSERIA-GONORRHOEAE PILUS MAPPED WITH ANTIBODIES
Autore:
FOREST KT; BERNSTEIN SL; GETZOFF ED; SO M; TRIBBICK G; GEYSEN HM; DEAL CD; TAINER JA;
Indirizzi:
SCRIPPS CLIN & RES FDN,RES INST,DEPT MOLEC BIOL LA JOLLA CA 92037 SCRIPPS CLIN & RES FDN,RES INST,DEPT MOLEC BIOL LA JOLLA CA 92037 CHIRON MIMOTOPES PTY LTD CLAYTON VIC 3168 AUSTRALIA
Titolo Testata:
Infection and immunity
fascicolo: 2, volume: 64, anno: 1996,
pagine: 644 - 652
SICI:
0019-9567(1996)64:2<644:AAAOTN>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSEUDOMONAS-AERUGINOSA PAK; AMINO-ACID-SEQUENCE; GONOCOCCAL PILI; PROTEIN; BINDING; VACCINE; IDENTIFICATION; NITROCELLULOSE; PURIFICATION; ADSORPTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
K.T. Forest et al., "ASSEMBLY AND ANTIGENICITY OF THE NEISSERIA-GONORRHOEAE PILUS MAPPED WITH ANTIBODIES", Infection and immunity, 64(2), 1996, pp. 644-652

Abstract

The relationship between the sequence of Neisseria gonorrhoeae pilin and its quaternary assembly into pilus fibers was studied with a set of site directed antibody probes and by mapping the specificities of antipilus antisera with peptides. Buried and exposed peptides in assembled pill were identified by competitive immunoassays and immunoelectronmicroscopy with polyclonal antibodies raised against 11 peptides spanning the pilin sequence. Pili did not compete significantly with pilinsubunits for binding to antibodies against residues 13 to 31 (13-31) and 18-36, Pilus fibers competed well with pilin protein subunits for binding to antibodies raised against peptides 37-56, 58-78, 110-120, 115-127, 122-139, and 140-159 and competed weakly for antibodies against residues 79-93 and 94-108, Antibodies to sequence-conserved residues37-56 and to semiconserved residues 94-108 preferentially bound pilusends as shown by immunoelectron microscopy. The exposure of pilus regions to the immune system was tested by peptide mapping of antiserum specificities against sets of overlapping peptides representing all possible hexameric or octameric peptides from the N. gonorrhoeae MS11 pilin sequence, The immunogenicity of exposed peptides incorporating semiconserved residues 49-56 and 121-126 was revealed by strong, consistent antigenic reactivity to these regions measured in antipilus sera from rabbits, mice, and humans and in sera from human volunteers with gonorrhea. The conservation and variation of antigenic responses among these three species clarify the relevance of immunological studies of other species to the human immune response against pathogens. Overall, our results explain the extreme conservation of the entire N-terminal one-third of the pilin protein by its dominant role in pilus assembly: hydrophobic residues 1-36 are implicated in buried lateral contacts, and polar residues 37-56 are implicated in longitudinal contacts withinthe pilus fiber.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:36:55