NDLI: Group B Streptococcus Pullulanase Crystal Structures in the Context of a Novel Strategy for Vaccine Development▿ †

Content Provider	PubMed Central
Author	Gourlay, Louise J. Santi, Isabella Alfredo, Pezzicoli Grandi, Guido Marco, Soriani Bolognesi, Martino
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 α-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 Å, respectively.
Related Links	http://dx.doi.org/10.1128/jb.01755-08
Ending Page	3552
Page Count	9
Starting Page	3544
File Format	PDF
ISSN	00219193
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	11
Volume Number	191
Language	English
Publisher	American Society for Microbiology (ASM)
Publisher Date	2009-06-01
Access Restriction	Open
Rights Holder	American Society for Microbiology (ASM)
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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