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Host cell membrane entry receptors are a broad class of surface molecules, including proteins, glycoproteins, and carbohydrates, that pathogens exploit to gain access to the intracellular environment. These receptors typically perform vital physiological functions, such as serving as chemokine receptors (e.g., CCR5), enzymes (e.g., ACE2), or adhesion molecules (e.g., ICAM-1), but are hijacked by viruses and bacteria through high-affinity interactions with pathogen-encoded ligands (Maginnis, 2018, Encyclopedia of Virology). For example, the SARS-CoV-2 spike protein binds to Angiotensin-converting enzyme 2 (ACE2) to trigger membrane fusion (Hoffmann et al., 2020, Cell), while HIV-1 utilizes CD4 and coreceptors like CCR5 or CXCR4 for entry (NIH, 2023). Therapeutic strategies targeting these host factors, such as the CCR5 antagonist Maraviroc, aim to block the initial stages of the infection cycle (Dorr et al., 2005, Antimicrob Agents Chemother). While host-targeted entry inhibitors can provide a high genetic barrier to pathogen resistance, they also carry risks of interfering with the receptor's endogenous biological roles, potentially leading to adverse effects or altered immune responses.
Inhibition of pathogen attachment, fusion, or entry by binding to host cell surface molecules and blocking interaction with pathogen ligands.
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