STRUCTURAL-PROPERTIES AND EVOLUTIONARY RELATIONSHIPS OF PSPA, A SURFACE PROTEIN OF STREPTOCOCCUS-PNEUMONIAE, AS REVEALED BY SEQUENCE-ANALYSIS

被引:175
作者
YOTHER, J
BRILES, DE
机构
[1] UNIV ALABAMA,DEPT PEDIAT,BIRMINGHAM,AL 35294
[2] UNIV ALABAMA,DEPT COMPARAT MED,BIRMINGHAM,AL 35294
关键词
D O I
10.1128/jb.174.2.601-609.1992
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Analysis of the sequence for the gene encoding PspA (pneumococcal surface protein A) of Streptococcus pneumoniae revealed the presence of four distinct domains in the mature protein. The structure of the N-terminal half of PspA was highly consistent with that of an alpha-helical coiled-coil protein. The alpha-helical domain was followed by a proline-rich domain (with two regions in which 18 of 43 and 5 of 11 of the residues are prolines) and a repeat domain consisting of 10 highly conserved 20-amino-acid repeats. A fourth domain consisting of a hydrophobic region too short to serve as a membrane anchor and a poorly charged region followed the repeats and preceded the translation stop codon. The C-terminal region of PspA did not possess features conserved among numerous other surface proteins, suggesting that PspA is attached to the cell by a mechanism unique among known surface proteins of gram-positive bacteria. The repeat domain of PspA was found to have significant homology with C-terminal repeat regions of proteins from Streptococcus mutans, Streptococcus downei, Clostridium difficile, and S. pneumoniae. Comparisons of these regions with respect to functions and homologies suggested that, through evolution, the repeat regions may have lost or gained a mechanism for attachment to the bacterial cell.
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页码:601 / 609
页数:9
相关论文
共 70 条
  • [51] STREPTOCOCCAL M-PROTEIN - ALPHA-HELICAL COILED-COIL STRUCTURE AND ARRANGEMENT ON THE CELL-SURFACE
    PHILLIPS, GN
    FLICKER, PF
    COHEN, C
    MANJULA, BN
    FISCHETTI, VA
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1981, 78 (08): : 4689 - 4693
  • [52] A DYE-BUOYANT-DENSITY METHOD FOR DETECTION AND ISOLATION OF CLOSED CIRCULAR DUPLEX DNA - CLOSED CIRCULAR DNA IN HELA CELLS
    RADLOFF, R
    BAUER, W
    VINOGRAD, J
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1967, 57 (05) : 1514 - &
  • [53] STREPTOCOCCUS-PYOGENES TYPE-12 M-PROTEIN GENE-REGULATION BY UPSTREAM SEQUENCES
    ROBBINS, JC
    SPANIER, JG
    JONES, SJ
    SIMPSON, WJ
    CLEARY, PP
    [J]. JOURNAL OF BACTERIOLOGY, 1987, 169 (12) : 5633 - 5640
  • [54] SEQUENCE OF THE STREPTOCOCCUS-PNEUMONIAE BACTERIOPHAGE-HB-3 AMIDASE REVEALS HIGH HOMOLOGY WITH THE MAJOR HOST AUTOLYSIN
    ROMERO, A
    LOPEZ, R
    GARCIA, P
    [J]. JOURNAL OF BACTERIOLOGY, 1990, 172 (09) : 5064 - 5070
  • [55] SHEFFIELD JS, UNPUB
  • [56] SHINE J, 1974, Proceedings of the National Academy of Sciences of the United States of America, V71, P1342, DOI 10.1073/pnas.71.4.1342
  • [57] SEQUENCE-ANALYSIS OF THE GTFB GENE FROM STREPTOCOCCUS-MUTANS
    SHIROZA, T
    UEDA, S
    KURAMITSU, HK
    [J]. JOURNAL OF BACTERIOLOGY, 1987, 169 (09) : 4263 - 4270
  • [58] AMINO-ACID SEQUENCE OF RABBIT SKELETAL TROPOMYOSIN AND ITS COILED COIL STRUCTURE
    SODEK, J
    HODGES, RS
    SMILLIE, LB
    JURASEK, L
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1972, 69 (12) : 3800 - 3804
  • [59] A 43-KILODALTON PNEUMOCOCCAL SURFACE PROTEIN, PSPA - ISOLATION, PROTECTIVE ABILITIES, AND STRUCTURAL-ANALYSIS OF THE AMINO-TERMINAL SEQUENCE
    TALKINGTON, DF
    CRIMMINS, DL
    VOELLINGER, DC
    YOTHER, J
    BRILES, DE
    [J]. INFECTION AND IMMUNITY, 1991, 59 (04) : 1285 - 1289
  • [60] TOMASZ A, 1981, REV INFECT DIS, V3, P190