Group B streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development.
J Bacteriol
; 191(11): 3544-52, 2009 Jun.
Article
em En
| MEDLINE
| ID: mdl-19329633
ABSTRACT
The group B streptococcus type I pullulanase (SAP) is a class 13 glycoside hydrolase that is anchored to the bacterial cell surface via a conserved C-terminal anchoring motif and involved in alpha-glucan degradation. Recent in vitro functional studies have shown that SAP is immunogenic in humans and that anti-SAP sera derived from immunized animals impair both group A and group B streptococcus pullulanase activities, suggesting that in vivo immunization with this antigen could prevent streptococcal colonization. To further investigate the putative role of SAP in bacterial pathogenesis, we carried out functional studies and found that recombinant SAP binds to human cervical epithelial cells. Furthermore, with a view of using SAP as a vaccine candidate, we present high-resolution crystal structure analyses of an N-terminally truncated form of SAP lacking the carbohydrate binding module but containing the catalytic domain and displaying glycosidase hydrolase activity, both in its apo form and in complex with maltotetraose, at resolutions of 2.1 and 2.4 A, respectively.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Streptococcus agalactiae
/
Modelos Moleculares
/
Cristalografia por Raios X
/
Glicosídeo Hidrolases
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
J Bacteriol
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Itália