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High molecular weight adhesin 1 (HMW1) is a prominent surface protein and a key virulence factor in non-typeable Haemophilus influenzae (NTHi), a major cause of respiratory tract infections in humans (St. Geme, 2002). It belongs to the two-partner secretion (TPS) family and is responsible for mediating the initial attachment of the bacteria to human respiratory epithelial cells, particularly through interaction with sialylated glycoprotein receptors (UniProt, P45989). This adhesion is a critical step in the colonization of the nasopharynx and the subsequent development of diseases such as otitis media, sinusitis, and exacerbations of chronic obstructive pulmonary disease (COPD) (Grass et al., 2003). HMW1 is post-translationally modified by glycosylation, which is necessary for its stability and functional conformation on the bacterial surface (Grass et al., 2003). As a highly immunogenic protein, HMW1 is a significant target for the development of vaccines and monoclonal antibodies aimed at preventing NTHi-related infections (St. Geme, 2002). However, the effectiveness of these therapies can be complicated by the genetic diversity and antigenic variation of HMW1 across different clinical isolates.
Inhibition of bacterial attachment to host respiratory epithelial cells to prevent colonization and infection (St. Geme, 2002).
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