Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens

被引:277
作者
Lindahl, G [1 ]
Stålhammar-Carlemalm, M [1 ]
Areschoug, T [1 ]
机构
[1] Lund Univ, Dept Med Microbiol Dermatol & Infect, SE-22362 Lund, Sweden
关键词
D O I
10.1128/CMR.18.1.102-127.2005
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Streptococcus agalactiae (group B Streptococcus) is the major cause of invasive bacterial disease, including meningitis, in the neonatal period. Although prophylactic measures have contributed to a substantial reduction in the number of infections, development of a vaccine remains an important goal. While much work in this field has focused on the S. agalactiae polysaccharide capsule, which is an important virulence factor that elicits protective immunity, surface proteins have received increasing attention as potential virulence factors and vaccine components. Here, we summarize current knowledge about S. agalactiae surface proteins, with emphasis on proteins that have been characterized immunochemically and/or elicit protective immunity in animal models. These surface proteins have been implicated in interactions with human epithelial cells, binding to extracellular matrix components, and/or evasion of host immunity. Of note, several S. agalactiae surface proteins are related to surface proteins identified in other bacterial pathogens, emphasizing the general interest of the S. agalactiae proteins. Because some S. agalactiae surface proteins elicit protective immunity they hold promise as components in a vaccine based only on proteins or as carriers in polysaccharide conjugate vaccines.
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页码:102 / +
页数:27
相关论文
共 271 条
[1]   Subtractive hybridization identifies a novel predicted protein mediating epithelial cell invasion by virulent serotype III group B Streptococcus agalactiae [J].
Adderson, EE ;
Takahashi, S ;
Wang, Y ;
Armstrong, J ;
Miller, DV ;
Bohnsack, JF .
INFECTION AND IMMUNITY, 2003, 71 (12) :6857-6863
[2]   Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes [J].
Anderson, ET ;
Wetherell, MG ;
Winter, LA ;
Olmsted, SB ;
Cleary, PP ;
Matsuka, YV .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (19) :4839-4851
[3]  
Areschoug T, 1999, INFECT IMMUN, V67, P6350
[4]   Host-pathogen interactions in Streptococcus pyogenes infections, with special reference to puerperal fever and a comment on vaccine development [J].
Areschoug, T ;
Carlsson, F ;
Stålhammar-Carlemalm, M ;
Lindahl, G .
VACCINE, 2004, 22 :S9-S14
[5]   A proline-rich region with a highly periodic sequence in streptococcal β protein adopts the polyproline II structure and is exposed on the bacterial surface [J].
Areschoug, T ;
Linse, S ;
Stålhammar-Carlemalm, M ;
Hedén, LO ;
Lindahl, G .
JOURNAL OF BACTERIOLOGY, 2002, 184 (22) :6376-6383
[6]   Streptococcal β protein has separate binding sites for human factor H and IgA-Fc [J].
Areschoug, T ;
Stålhammar-Carlemalm, M ;
Karlsson, I ;
Lindahl, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (15) :12642-12648
[7]   Immune response of healthy women to 2 different group B streptococcal type V capsular polysaccharide-protein conjugate vaccines [J].
Baker, CJ ;
Paoletti, LC ;
Rench, MA ;
Guttormsen, HK ;
Edwards, MS ;
Kasper, DL .
JOURNAL OF INFECTIOUS DISEASES, 2004, 189 (06) :1103-1112
[8]   Group B streptococcal conjugate vaccines [J].
Baker, CJ ;
Edwards, MS .
ARCHIVES OF DISEASE IN CHILDHOOD, 2003, 88 (05) :375-378
[9]   CORRELATION OF MATERNAL ANTIBODY DEFICIENCY WITH SUSCEPTIBILITY TO NEONATAL GROUP-B STREPTOCOCCAL INFECTION [J].
BAKER, CJ ;
KASPER, DL .
NEW ENGLAND JOURNAL OF MEDICINE, 1976, 294 (14) :753-756
[10]   Structure and distribution of an unusual chimeric genetic element encoding macrolide resistance in phylogenetically diverse clones of group A Streptococcus [J].
Banks, DJ ;
Porcella, SF ;
Barbian, KD ;
Martin, JM ;
Musser, JM .
JOURNAL OF INFECTIOUS DISEASES, 2003, 188 (12) :1898-1908