Patrick O. Byrne

Structure-based design of soluble prefusion-stabilized herpes simplex virus type 2 glycoprotein B antigens

This study designs prefusion-stabilized HSV-2 gB antigens using structure-based methods and evaluates their immunogenicity, finding no improvement in neutralizing antibody titers compared to postfusion constructs.

Design, Structure, and Immunogenicity of a Soluble Prefusion-stabilized EBV gB Antigen

This study designs and characterizes a prefusion-stabilized EBV gB antigen, showing improved immunogenicity and structural insights for vaccine development.

A human cytomegalovirus prefusion-like glycoprotein B subunit vaccine elicits similar humoral immunity to that of postfusion gB in mice

This study compares humoral immunity elicited by prefusion-like and postfusion forms of HCMV gB in mice, finding similar neutralization titers but differences in antibody binding and phagocytosis.

Structure-based design of a soluble human cytomegalovirus glycoprotein B antigen stabilized in a prefusion-like conformation

This paper describes the stabilization of HCMV gB in a prefusion-like conformation using structure-based design and shows similar neutralizing antibody titers against postfusion and prefusion forms.

Structural basis for antibody recognition of vulnerable epitopes on Nipah virus F protein

This study identifies eight neutralization-sensitive epitopes on Nipah virus F protein using monoclonal antibodies and cryo-electron microscopy, four of which are novel.

Activity of EGFR transmembrane region variants indicates specific transmembrane dimers are not required for EGFR activity

The paper investigates the role of specific transmembrane dimers in EGFR activity and finds that many transmembrane sequences are compatible with EGFR function without requiring specific dimer conformations.