Bacterial neuraminidase (BNA)

Bacterial neuraminidases, also known as sialidases, are enzymes secreted by a wide range of pathogenic bacteria, including Streptococcus pneumoniae, Vibrio cholerae, and Pseudomonas aeruginosa (Source: PubMed, PMID: 24034729). These enzymes function by cleaving terminal sialic acid residues from host cell surface glycoproteins and glycolipids, which facilitates bacterial adherence, colonization, and tissue invasion (Source: UniProt, EC 3.2.1.18). By removing sialic acids, these enzymes also provide a nutrient source for the bacteria and help mask the pathogen from the host immune system by altering cell surface patterns (Source: PMC, PMC4153838). In clinical contexts, bacterial neuraminidases are significant virulence factors contributing to diseases such as pneumonia, meningitis, and sepsis (Source: PubMed, PMID: 30254101). While viral neuraminidase inhibitors like oseltamivir and zanamivir are primarily designed for influenza, they have shown varying degrees of cross-inhibitory activity against certain bacterial sialidases (Source: PubMed, PMID: 21859280). Current research focuses on developing potent and selective bacterial neuraminidase inhibitors as a form of anti-virulence therapy to mitigate infection severity and combat antibiotic resistance.

Other names

SialidaseExo-alpha-sialidaseN-acetylneuraminate glycohydrolaseNanANanBNanHVibrio cholerae neuraminidase (VCN)Pseudomonas aeruginosa neuraminidase (PaN)

Competitive inhibition of the enzyme's active site, preventing the catalytic cleavage of terminal sialic acid residues from host glycoconjugates to disrupt bacterial colonization and nutrient uptake.