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Cryptosporidium parvum surface antigens are a diverse group of proteins and glycoproteins located on the outer membrane of the parasite's life stages, particularly sporozoites and merozoites. These antigens, such as GP60 (cleaved into GP40 and GP15), P23, and GP900, play critical roles in the parasite's life cycle, including excystation, gliding motility, and attachment to and invasion of host intestinal epithelial cells (O'Connor et al., 2007; Perryman et al., 1996). Because they are exposed to the host immune system, they are primary targets for the development of vaccines, passive immunotherapy (e.g., hyperimmune bovine colostrum), and monoclonal antibodies aimed at neutralizing the parasite and preventing infection (Tzipori and Ward, 2002). In clinical practice, these antigens also serve as the basis for diagnostic assays, such as enzyme-linked immunosorbent assays (ELISA) and immunochromatographic tests used to detect C. parvum in fecal samples (Garcia et al., 2003). The high degree of polymorphism in some of these antigens, particularly GP60, poses a challenge for broad-spectrum therapeutic and vaccine development (Strong et al., 2000). Cryptosporidiosis remains a significant cause of diarrheal disease, particularly in resource-limited settings and among immunocompromised populations (Checkley et al., 2015).
Neutralization of parasite infectivity by blocking attachment and invasion of host enterocytes (Tzipori and Ward, 2002).
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