Exo-alpha-sialidase (NanH) (NanH)

Sialidase NanH is a bacterial exo-enzyme that catalyzes the hydrolysis of terminal sialic acid residues from host glycoconjugates such as glycoproteins and glycolipids (UniProt P0C0S1). It is a major virulence factor in various pathogenic bacteria, including Clostridium perfringens, Vibrio cholerae, and Gardnerella vaginalis, where it facilitates colonization, nutrient acquisition, and biofilm formation (PubMed 25663131). By stripping sialic acids from the host cell surface, NanH can unmask receptors for bacterial toxins or adhesins and modulate the host's innate immune response (PubMed 21844318). In clinical contexts, NanH activity is often used as a diagnostic marker for conditions like bacterial vaginosis, where it contributes to the degradation of the protective mucus layer (PubMed 30254014). Therapeutic strategies targeting NanH focus on small-molecule inhibitors, such as transition-state analogs like 2,3-dehydro-2-deoxy-N-acetylneuraminic acid (DANA), to attenuate bacterial pathogenicity (PubMed 25663131). Although most commercial neuraminidase inhibitors are designed for influenza viruses, NanH represents a distinct target for developing narrow-spectrum or broad-spectrum anti-bacterial agents (PubMed 30254014).

Other names

NeuraminidaseSialidaseN-acetylneuraminate glycohydrolaseExo-alpha-2,3-sialidaseNanH sialidase

Competitive inhibition of the sialidase enzyme activity, preventing the cleavage of terminal sialic acids from host cell surfaces and glycoconjugates.