Antigenicity, expression, and molecular characterization of surface-located pullulanase of Streptococcus pneumoniae

被引：28

作者：

Bongaerts, RJM ^{[1
]}

Heinz, HP ^{[1
]}

Hadding, U ^{[1
]}

Zysk, G ^{[1
]}

机构：

[1] Univ Dusseldorf, Dept Med Microbiol & Virol, D-40225 Dusseldorf, Germany

来源：

INFECTION AND IMMUNITY | 2000年 / 68卷 / 12期

关键词：

D O I：

10.1128/IAI.68.12.7141-7143.2000

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

A putative pullulanase-encoding gene from Streptococcus pneumoniae was identified by screening a genomic expression library with human convalescent-phase serum. The 3,864-bp gene encoded a 143-kDa protein. Surface location and pullulanase activity of the protein, designated SpuA, was demonstrated. SpuA was present in all investigated pneumococcal isolates of different serotypes. The spruA 5' end was highly conserved among clinical isolates except for a 75-bp region. The properties of SpuA reported here indicate that this novel immunogenic surface protein might have potential as a vaccine target.

引用

页码：7141 / 7143

页数：3

共 10 条

[1] Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus [J].

Albertson, GD ;

McHale, RH ;

Gibbs, MD ;

Bergquist, PL .

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 1997, 1354 (01) :35-39

[2] Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins [J].

Bateman, A ;

Birney, E ;

Durbin, R ;

Eddy, SR ;

Finn, RD ;

Sonnhammer, ELL .

NUCLEIC ACIDS RESEARCH, 1999, 27 (01) :260-262

[3] Gene knockout of the intracellular amylase gene by homologous recombination in Streptococcus bovis [J].

Brooker, JD ;

McCarthy, JM .

CURRENT MICROBIOLOGY, 1997, 35 (03) :133-138

[4] CONSERVATION OF A HEXAPEPTIDE SEQUENCE IN THE ANCHOR REGION OF SURFACE-PROTEINS FROM GRAM-POSITIVE COCCI [J].

FISCHETTI, VA ;

PANCHOLI, V ;

SCHNEEWIND, O .

MOLECULAR MICROBIOLOGY, 1990, 4 (09) :1603-1605

[5] Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes alpha-1,4 and alpha-1,6 linkages in polysaccharides at different active sites [J].

Hatada, Y ;

Igarashi, K ;

Ozaki, K ;

Ara, K ;

Hitomi, J ;

Kobayashi, T ;

Kawai, S ;

Watabe, T ;

Ito, S .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (39) :24075-24083

[6] IDENTIFICATION OF AN ENDOGENOUS MEMBRANE ANCHOR-CLEAVING ENZYME FOR GROUP-A STREPTOCOCCAL M-PROTEIN - ITS IMPLICATION FOR THE ATTACHMENT OF SURFACE-PROTEINS IN GRAM-POSITIVE BACTERIA [J].

PANCHOLI, V ;

FISCHETTI, VA .

JOURNAL OF EXPERIMENTAL MEDICINE, 1989, 170 (06) :2119-2133

[7] Application of the extracellular alpha-amylase gene from Streptococcus bovis 148 to construction of a secretion vector for yogurt starter strains [J].

Satoh, E ;

Ito, Y ;

Sasaki, Y ;

Sasaki, T .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1997, 63 (11) :4593-4596

[8] STRUCTURE OF THE CELL-WALL ANCHOR OF SURFACE-PROTEINS IN STAPHYLOCOCCUS-AUREUS [J].

SCHNEEWIND, O ;

FOWLER, A ;

FAULL, KF .

SCIENCE, 1995, 268 (5207) :103-106

[9] Pfam: multiple sequence alignments and HMM-profiles of protein domains [J].

Sonnhammer, ELL ;

Eddy, SR ;

Birney, E ;

Bateman, A ;

Durbin, R .

NUCLEIC ACIDS RESEARCH, 1998, 26 (01) :320-322

[10] Detection of 23 immunogenic pneumococcal proteins using convalescent-phase serum [J].

Zysk, G ;

Bongaerts, RJM ;

Ten Thoren, E ;

Bethe, G ;

Hakenbeck, R ;

Heinz, HP .

INFECTION AND IMMUNITY, 2000, 68 (06) :3740-3743

← 1 →