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Lectin activity of Pseudomonas aeruginosa vaccine candidates PSE17-1, PSE41-5 and PSE54
Christopher J Day1, Lauren E Hartley-Tassell1, Kate L Seib1
1Institute for Glycomics, Griffith University, Gold Coast, QLD, 4222, Australia.
Insights
Three new Pseudomonas aeruginosa surface proteins (PSE17-1, PSE41-5, PSE54) were identified as novel lectins. These proteins bind to host cell glycans, suggesting potential roles in Pseudomonas aeruginosa infections, particularly in cystic fibrosis patients.
Area of Science:
- Microbiology
- Immunology
- Glycobiology
Background:
- Pseudomonas aeruginosa is an opportunistic pathogen causing infections in immunocompromised individuals, including cystic fibrosis (CF) patients.
- Known P. aeruginosa lectins (PA-IL, PA-IIL) mediate adherence to host cells, especially in CF airways.
- Novel surface proteins identified via reverse vaccinology warrant investigation for their roles in host-pathogen interactions.
Purpose of the Study:
- To identify and characterize novel glycan-binding proteins (lectins) of Pseudomonas aeruginosa.
- To investigate the binding specificities of newly identified P. aeruginosa surface proteins (PSE17-1, PSE41-5, PSE54) to human cell glycans.
- To assess the potential role of these novel lectins in P. aeruginosa infection.
Main Methods:
- Screening of novel P. aeruginosa surface proteins (PSE17-1, PSE41-5, PSE54) for glycan binding using glycan arrays.
- Confirmation of lectin activity and affinity determination using surface plasmon resonance (SPR).
- Analysis of binding specificities against a panel of human cell-associated glycans.
Main Results:
- Three novel lectins, PSE17-1, PSE41-5, and PSE54, were identified in P. aeruginosa.
- These proteins exhibit nanomolar affinities for various host glycans.
- PSE17-1 binds hyaluronic acid and sialyl Lewis A/X; PSE41-5 binds β-linked galactose and Lewis/ABO antigens; PSE54 binds ABO antigens and β-linked galactose.
Conclusions:
- PSE17-1, PSE41-5, and PSE54 are novel P. aeruginosa lectins with defined glycan-binding specificities.
- These lectins likely contribute to P. aeruginosa adherence and infection of host cells.
- The identified lectins represent potential targets for therapeutic or vaccine development against P. aeruginosa infections.
Abstract:
Pseudomonas aeruginosa is an opportunistic pathogen that causes nosocomial infections most commonly in immunocompromised, cystic fibrosis (CF) and burns patients. The pilin and Pseudomonas lectins 1 (PA-IL) and 2 (PA-IIL) are known glycan-binding proteins of P. aeruginosa that are involved in adherence to host cells, particularly CF host airways. Recently, new P. aeruginosa surface proteins were identified by reverse vaccinology and tested in vivo as potential vaccine antigens. Three of these, namely PSE17-1, PSE41-5 and PSE54, were screened for glycan binding using glycan arrays displaying glycan structures representative of those found on human cells. Surface plasmon resonance was used to confirm the lectin activity of these proteins, and determined affinities with several host glycans to be in the nanomolar range. PSE17-1 binds hyaluronic acid and sialyl Lewis A and X. PSE41-5 binds terminal β-linked galactose structures, Lewis and ABO blood group antigens. PSE54 binds to ABO blood group antigens and some terminal β-linked galactose. All three proteins are novel lectins of P. aeruginosa with potential roles in infection of host cells.
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