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In tropical and subtropical countries, dengue virus (DENV) infections have been increasing; however, we still lack effective therapy. In the present study, we aimed to engineer a bispecific antibody (subsequently named LUZ-8F2–6B1), based on monoclonal antibody 6B1, which has anti DENV-1, 2, and 3 activity, and 8F2, which has anti DENV-4 activity. LUZ-8F2–6B1 displayed potent neutralization activity against four serotypes of DENV by binding to the envelop protein. In vivo , we demonstrated that LUZ-8F2–6B1 could provide protection against infection by four serotypes of DENV in a mouse model. In addition, the deletion of nine amino acids in the Fc region (LUZ-8F2–6B1-9del) completely abolished the antibody-dependent enhancement observed at lower doses of the antibody. Thus, LUZ-8F2–6B1 is a promising, safe, and effective agent for the prophylaxis and treatment of DENV infection. • An engineered bispecific antibody LUZ-8F2-6B1 showed potent neutralization activity against all four serotypes of DENV. • In vivo, a mouse model showed that LUZ-8F2-6B1 provided protection against infection by all four serotypes of DENVs. • LUZ-8F2-6B1-9del completely abrogated antibody dependent enhancement, which occurs when using lower doses of the antibody. • LUZ-8F2-6B1 could be an effective and safe agent for the prophylaxis and therapy of DENV infection. [ABSTRACT FROM AUTHOR]

Human adenovirus serotype 7 (HAdV-7), belonging to species B, has caused severe lower respiratory tract diseases and even deaths recently. However, no adenovirus vaccine or therapeutic is available thus far. In this study, a HAdV-7-specific human monoclonal antibody (HMAb), 3-3E, isolated from single plasma cells obtained from the peripheral blood mononuclear cells of HAdV-7-infected patients showed potent HAdV-7 neutralization activity. The results showed HMAb 3-3E only binds to the hexon protein of intact HAdV-7 or the recombinant hexon protein and it does not bind to other intact virion particles. This could mean the antibody recognizes a conformational epitope of the hexon protein. Further, HMAb 3-3E potently neutralized HAdV-7 in vitro at low concentrations. In vivo studies showed HMAb 3-3E protected from HAdV-7 infection in a murine model. Therefore, HMAb 3-3E is promising as a safe and effective prophylactic and therapeutic treatment for HAdV-7 infection. [ABSTRACT FROM AUTHOR]