Pneumococcal surface protein A (PspA) is serologically highly variable and is expressed by all clinically important capsular serotypes of Streptococcus pneumoniae

Crain, Marilyn J.; Waltman, W. D.; Turner, Joshua; Yother, Janet; Talkington, Deborah F.; McDaniel, Larry S.; Gray, Barry M.; Briles, David E.

doi:10.1128/iai.58.10.3293-3299.1990

Cited by 237 publications

(116 citation statements)

References 16 publications

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“…The speci¢city was determined by immunoblot and dot blot reaction patterns against pneumococci and other Gram-positive bacteria as well as Gram-negative bacteria. The mAb 180,C-1 showed several bands in each reacting strain and a strain to strain variation in the molecular size of PspA ; in accordance with what is reported for other mAbs against this protein [17]. Because PspA is an antigenically variable protein [17], the epitope for mAb 180,C-1 was detected in only 19 out of 76 examined S. pneumoniae strains.…”

Section: Monoclonal Antibodiessupporting

confidence: 86%

“…The mAb 180,C-1 showed several bands in each reacting strain and a strain to strain variation in the molecular size of PspA ; in accordance with what is reported for other mAbs against this protein [17]. Because PspA is an antigenically variable protein [17], the epitope for mAb 180,C-1 was detected in only 19 out of 76 examined S. pneumoniae strains. The negative control mAb 184,F-12 (IgG3) reacts with the P1.16 epitope on meningococcal class 1 protein [18].…”

Section: Monoclonal Antibodiessupporting

confidence: 86%

“…The ¢nding that the bands detected by mAb 180,C-1 showed the same mobility as some of the high molecular mass proteins reactive with the human sera could indicate that PspA was co-puri¢ed with hsp70 in the presence of Triton. The high molecular mass immunoreactive proteins were not detected by all human sera, and a possible explanation for this could be that PspA is an antigenically variable protein [17].…”

Section: Pspa Seems To Be Co-puri¢ed With Hsp70mentioning

confidence: 92%

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Streptococcus pneumoniae heat shock protein 70 does not induce human antibody responses during infection

Kolberg¹

2000

FEMS Immunology and Medical Microbiology

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Mouse monoclonal antibodies (mAbs) were developed against Streptococcus pneumoniae in search for potential common pneumococcal proteins as vaccine antigens. mAb 230,B-9 (IgG1) reacted by immunoblotting with a 70-kDa protein which was isolated by immunoaffinity chromatography and subsequent preparative electrophoresis. N-terminal amino acid sequencing showed homology to that of heat shock protein 70 (hsp70). The hsp70 epitope reactive with mAb 230,B-9 was found in all the pneumococci examined as well as in other streptococci and enterococci. The epitope was not expressed in several other examined Gram-positive or -negative bacteria. Pneumococcal hsp70 has by other investigators been proposed to be a vaccine candidate. Binding experiments using flow cytometry showed that the epitope was not surface-exposed on live exponential phase grown S. pneumoniae. Human patient sera did not react with affinity-purified pneumococcal hsp70. Therefore the pneumococcal hsp70 does not seem to be of special interest in a vaccine formulation. The human sera contained antibodies to high molecular proteins co-purified with hsp70. Some of these proteins could be the pneumococcal surface protein A.

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Section: Monoclonal Antibodiessupporting

confidence: 86%

Section: Monoclonal Antibodiessupporting

confidence: 86%

Section: Pspa Seems To Be Co-puri¢ed With Hsp70mentioning

confidence: 92%

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Streptococcus pneumoniae heat shock protein 70 does not induce human antibody responses during infection

Kolberg¹

2000

FEMS Immunology and Medical Microbiology

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“…Among the pneumococcal proteins identified as potential vaccine antigens, the pneumococcal surface protein A (PspA) and the pneumococcal surface adhesin A (PsaA) are promising candidates. PspA inhibits complement deposition on pneumococci [5], is essential for full virulence of pneumococci [6], and is present on all clinically important pneumococcal strains [7]. Immunization with a recombinant PspA derived from strain Rx1 has been shown to be safe and to induce a broadly cross-reactive immune response in humans [3].…”

Section: Introductionmentioning

confidence: 99%

Natural materno-fetal transfer of antibodies to PspA and to PsaA

Baril¹,

Briles

Crozier³

et al. 2004

Clinical and Experimental Immunology

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SUMMARYPspA and PsaA are Streptococcus pneumoniae surface proteins and potential pneumococcal vaccine antigens. The aim of this study was to characterize the transplacental transfer of antibodies to PspA and to PsaA. Paired mother and cord blood sera were obtained at delivery from 28 women. Concentrations of antibodies against PspA, PsaA, tetanus toxoid (vaccine-induced antibodies) and P6-outer membrane protein (OMP) of nontypeable Haemophilus influenzae were determined by ELISA. Antibodies to PspA of the IgG, IgG1 and IgG2 antibodies were also determined. The geometric mean percentage (GM%) of the paired infant:mother antibody were calculated. Results: The GM% of the infant:mother antibody concentrations against PspA, PsaA and P6-OMP antibodies were 64·7% (3·3 m g/ml in infants vs. 5·1 m g/ml in mothers), 50·4% (6·8 m g/ml vs. 13·5 m g/ml) and 66·7% (5·6 m g/ml vs. 8·4 m g/ml), respectively; the GM% of antibodies against tetanus toxoid was 104·5% (4·6 m g/ml vs. 4·4 m g/ml). Transplacental transfer of IgG1 was more efficient than that of IgG2 (approximately 120% vs. 65%). A transplacental transfer of antibodies to PspA and to PsaA exist. Moreover, these data suggest an active placental transfer of IgG1 antibodies to PspA since the concentration of these antibodies were consistently higher in cord sera than in the mother's sera.

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“…mAbs are useful tools for such analyses. PspA has been identi¢ed by over 12 mAbs [10], but these mAbs are raised against a few strains [14,15]. Most of the mAbs were produced after immunisation of XiD (X-linked immunode¢cient CBA/ N) mice which do not make antibodies to polysaccharide antigens.…”

Section: Introductionmentioning

confidence: 99%

Epitope analyses of pneumococcal surface protein A: a combination of two monoclonal antibodies detects 94% of clinical isolates

Kolberg¹

2001

FEMS Immunology and Medical Microbiology

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Immunisation of BALB/c mice with seven heat-treated Norwegian clinical isolates of Streptococcus pneumoniae of different serotypes elicited mainly monoclonal antibodies (mAbs) to pneumococcal surface protein A (PspA). It was remarkable that the fusions resulted only in a few mAbs directed against other protein antigens. Dot blot analysis with 16 mAbs using clinical isolates representing 23 different capsular types and the uncapsulated reference strain R36A showed that some of the mAbs bound to PspA epitopes expressed by a low number of strains whereas others bound to broadly distributed epitopes. On the basis of their reactivities, seven of these mAbs could be divided into two groups recognising different subsets of pneumococci. The three mAbs in the narrow reacting group bound to epitopes found in 21-25% of the strains whereas the four mAbs in the broad reacting group detected more than 57% of the analysed strains. The epitopes for these seven antibodies were surface exposed on live exponential phase grown pneumococci as shown by flow cytometry. The finding that a combination of mAb 180,C-1 (IgG2a) from the first group and mAb 170,E-11 (IgG2a) from the second group detected 94% of the examined strains is interesting because PspA has been reported by others to be a serological highly variable protein.

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Pneumococcal surface protein A (PspA) is serologically highly variable and is expressed by all clinically important capsular serotypes of Streptococcus pneumoniae

Cited by 237 publications

References 16 publications

Streptococcus pneumoniae heat shock protein 70 does not induce human antibody responses during infection

Streptococcus pneumoniae heat shock protein 70 does not induce human antibody responses during infection

Natural materno-fetal transfer of antibodies to PspA and to PsaA

Epitope analyses of pneumococcal surface protein A: a combination of two monoclonal antibodies detects 94% of clinical isolates

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