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Human cytomegalovirus glycoprotein B (gB) is a highly conserved envelope protein essential for viral membrane fusion and entry. It acts as a class III viral fusogen and is the principal target of neutralizing antibodies, though most antibodies raised are non-neutralizing due to extensive glycan shielding on neutralizing epitopes[1][2][3][4]. It is central to vaccine antigen design and correlates with protection when vaccine-induced IgG binds native gB[4]. HCMV pp65–IE1 fusion protein is a recombinant antigen combining pp65 (the major matrix phosphoprotein and dominant target of T cell responses) with IE1 (the principal immediate-early transcriptional transactivator). This fusion is not a natural protein but is widely used in vaccines and T cell therapy research to optimize induction of cellular immunity against CMV. Both are commonly combined in multi-antigen vaccines and immunotherapies for preventing CMV infection or reactivation, especially in high-risk populations like transplant recipients and the congenitally infected[4][5]. Note: The entry "CMV glycoprotein B and CMV pp65–IE1 fusion protein" is not a single molecular entity but a combination of two antigens used synergistically in immunological approaches to CMV. For detailed structural or drug-target annotation, these should be split. However, this combination is standard for vaccine and immunotherapy literature. Summary: - Both gB and pp65–IE1 fusion are therapeutic and research targets against CMV infection. - gB is a viral fusion protein; pp65–IE1 fusion is used to elicit T cell responses. - Both are critical for immune protection, but "CMV glycoprotein B and CMV pp65–IE1 fusion protein" is a combined immunogen, not a natural molecule[1][2][4][5].
gB-targeting: Elicits neutralizing antibodies that block viral entry and fusion pp65–IE1 fusion-targeting: Stimulates cytotoxic T lymphocytes (CTLs) to recognize and destroy infected cells Both: Immunization aiming for protection via antibody (gB) and cellular immunity (pp65/IE1)
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