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Pneumococcal surface adhesin A (PsaA): a review.

Gowrisankar Rajam¹, Julie M Anderton, George M Carlone

¹Division of Bacterial Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30333, USA.

Critical Reviews in Microbiology

|September 27, 2008

Summary

Pneumococcal surface adhesin A (PsaA) is a key Streptococcus pneumoniae protein. Evaluating PsaA as a vaccine component shows potential to reduce bacterial colonization and combat pneumococcal disease.

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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

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Published on: October 2, 2017

Area of Science:

Microbiology
Immunology
Vaccinology

Background:

Pneumococcal surface adhesin A (PsaA) is a conserved lipoprotein found in all Streptococcus pneumoniae serotypes.
PsaA functions as both a Mn(2+) transporter and a crucial adhesin for bacterial attachment and virulence.
Natural infection with pneumococci induces an antibody response against PsaA, indicating its immunogenicity.

Purpose of the Study:

To review the structure, function, and immunogenicity of PsaA.
To evaluate PsaA's potential as a vaccine candidate against pneumococcal infections.
To assess PsaA's role in reducing nasopharyngeal colonization, a critical step in pneumococcal pathogenesis.

Main Methods:

Review of existing literature on PsaA.
Expression and purification of recombinant PsaA in E. coli.
Evaluation of PsaA in a phase one clinical trial.

Main Results:

PsaA is a multi-functional lipoprotein essential for pneumococcal attachment and virulence.
PsaA elicits an immune response, with antibodies increasing during natural colonization.
Recombinant PsaA has been successfully produced and tested in early-stage human trials.

Conclusions:

PsaA is a promising target for vaccine development due to its conserved nature and role in virulence.
PsaA-based vaccines could potentially reduce nasopharyngeal colonization and prevent pneumococcal disease.
Further evaluation of PsaA as a common antigen vaccine component is warranted.