Variation in the molecular weight of PspA (pneumococcal surface protein A) among Streptococcus pneumoniae

Waltman, W. D.; McDaniel, Larry S.; Gray, Barry M.; Briles, David E.

doi:10.1016/0882-4010(90)90008-e

Cited by 49 publications

(33 citation statements)

References 13 publications

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“…The differences in efficiency of PspA release among S. pneumoniae strains may reflect either different cell surface properties or variability in the PspAs. PspAs from different strains exhibit both serologic and molecular weight variabilities (14,42,43,64); the latter are apparently due to size variation in both the N-and C-terminal halves of the molecule (67).…”

Section: Discussionmentioning

confidence: 99%

Novel surface attachment mechanism of the Streptococcus pneumoniae protein PspA

1994

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Pneumococcal surface protein A (PspA) of Streptococcus pneumoniae has been found to utilize a novel mechanism for anchoring to the bacterial cell surface. In contrast to that of surface proteins from other gram-positive bacteria, PspA anchoring required choline-mediated interactions between the membrane-associated lipoteichoic acid and the C-terminal repeat region of PspA. Release of PspA from the cell surface could be effected by deletion of 5 of the 10 C-terminal repeat units, by high concentrations of choline, or by growth in choline-deficient medium. Other pneumococcal proteins, including autolysin, which has a similar C-terminal repeat region, were not released by these treatments. The attachment mechanism utilized by PspA thus appears to be uniquely adapted to exploit the unusual structure of the pneumococcal cell surface. Further, it has provided the means for rapid and simple isolation of immunogenic PspA from S. pneumoniae.

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Section: Discussionmentioning

confidence: 99%

Novel surface attachment mechanism of the Streptococcus pneumoniae protein PspA

1994

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“…PspA is a surface protein with variable molecular size ranging from 67 to 99 kDa (161). Based on sequence analysis, the protein has four distinct domains: an N-terminal highly charged ␣-helical region (288 amino acids in strain Rx1), a proline-rich domain (83 amino acids), a stretch of 10 highly conserved 20-amino-acid repeats, and a tail of 17 slightly hydrophobic residues at the C terminus (166).…”

Section: Pneumococcal Surface Protein Amentioning

confidence: 99%

Pneumococcal Virulence Factors: Structure and Function

Jedrzejas

2001

Microbiol Mol Biol Rev

407

354

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The overall goal for this review is to summarize the current body of knowledge about the structure and function of major known antigens of Streptococcus pneumoniae, a major gram-positive bacterial pathogen of humans. This information is then related to the role of these proteins in pneumococcal pathogenesis and in the development of new vaccines and/or other antimicrobial agents. S. pneumoniae is the most common cause of fatal community-acquired pneumonia in the elderly and is also one of the most common causes of middle ear infections and meningitis in children. The present vaccine for the pneumococcus consists of a mixture of 23 different capsular polysaccharides. While this vaccine is very effective in young adults, who are normally at low risk of serious disease, it is only about 60% effective in the elderly. In children younger than 2 years the vaccine is ineffective and is not recommended due to the inability of this age group to mount an antibody response to the pneumococcal polysaccharides. Antimicrobial drugs such as penicillin have diminished the risk from pneumococcal disease. Several pneumococcal proteins including pneumococcal surface proteins A and C, hyaluronate lyase, pneumolysin, autolysin, pneumococcal surface antigen A, choline binding protein A, and two neuraminidase enzymes are being investigated as potential vaccine or drug targets. Essentially all of these antigens have been or are being investigated on a structural level in addition to being characterized biochemically. Recently, three-dimensional structures for hyaluronate lyase and pneumococcal surface antigen A became available from X-ray crystallography determinations. Also, modeling studies based on biophysical measurements provided more information about the structures of pneumolysin and pneumococcal surface protein A. Structural and biochemical studies of these pneumococcal virulence factors have facilitated the development of novel antibiotics or protein antigen-based vaccines as an alternative to polysaccharide-based vaccines for the treatment of pneumococcal disease

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“…Its size is straindependent and varies from ϳ67 to 99 kDa (15). It is attached to pneumococci through noncovalent interactions of the C-terminal repeat region with the terminal choline residues of the teichoic or lipoteichoic acids present on the pneumococcal cell wall (16) and classified as a choline-binding protein.…”

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confidence: 99%

Characterization of Selected Strains of Pneumococcal Surface Protein A

Jedrzejas¹,

Lamani²,

Becker³

2001

Journal of Biological Chemistry

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Several proteins, in addition to the polysaccharide capsule, have recently been implicated in the full virulence of the Streptococcus pneumoniae bacterial pathogen. One of these novel virulence factors of S. pneumoniae is pneumococcal surface protein A (PspA). The N-terminal, cell surface exposed, and functional part of PspA is essential for full pneumococcal virulence, as evidenced by the fact that antibodies raised against this part of the protein are protective against pneumococcal infections. PspA has recently been implicated in anticomplementary function as it reduces complement-mediated clearance and phagocytosis of pneumococci. Several recombinant N-terminal fragments of PspA from different strains of pneumococci, Rx1, BG9739, BG6380, EF3296, and EF5668, were analyzed using circular dichroism, analytical ultracentrifugation sedimentation velocity and equilibrium methods, and sequence homology. Uniformly, all strains of PspA molecules studied have a high ␣-helical secondary structure content and they adopt predominantly a coiled-coil structure with an elongated, likely rod-like shape. No ␤-sheet structures were detected for any of the PspA molecules analyzed. All PspAs were found to be monomeric in solution with the exception of the BG9739 strain which had the propensity to partially aggregate but only into a tetrameric form. These structural properties were correlated with the functional, anti-complementary properties of PspA molecules based on the polar distribution of highly charged termini of its coiled-coil domain. The recombinant Rx1 PspA is currently under consideration for pneumococcal vaccine development.

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Variation in the molecular weight of PspA (pneumococcal surface protein A) among Streptococcus pneumoniae

Cited by 49 publications

References 13 publications

Novel surface attachment mechanism of the Streptococcus pneumoniae protein PspA

Novel surface attachment mechanism of the Streptococcus pneumoniae protein PspA

Pneumococcal Virulence Factors: Structure and Function

Characterization of Selected Strains of Pneumococcal Surface Protein A

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