What is the clinical evidence from this study?

Study design: Other. Population: Human metapneumovirus (hMPV). Intervention: Postfusion hMPV B2 F protein. Primary outcome: Immunogenicity and protective efficacy.

June 23, 2021Open Access

Structure, Immunogenicity, and Conformation-Dependent Receptor Binding of the Postfusion Human Metapneumovirus F Protein

JHJiachen HuangScripps Research Institute PCPradeep ChopraUniversity of Georgia LLLin LiuChengdu University of Traditional Chinese Medicine

Key Result

Vaccination with the postfusion hMPV B2 F protein generated a balanced Th1/Th2 response and targeted two previously discovered neutralizing epitopes.

Structured PICO

Population

Preclinical models (in vitro and vaccination models) for human metapneumovirus (hMPV)

Intervention

Postfusion hMPV B2 F protein (structural analysis and vaccination)

Outcome

X-ray crystal structure, binding to heparin and heparan sulfate, immunogenicity, and protective efficacysurrogate

The structural and immunogenic characterization of the postfusion hMPV F protein provides foundational knowledge for vaccine development against human metapneumovirus.

Abstract

Human metapneumovirus (hMPV) is an important cause of viral respiratory disease. In this paper, we report the X-ray crystal structure of the hMPV fusion (F) protein in the postfusion conformation from genotype B. We also assessed binding of the hMPV F protein to heparin and heparan sulfate, a previously reported receptor for the hMPV F protein. Furthermore, we determined the immunogenicity and protective efficacy of postfusion hMPV B2 F protein, which is the first study using a homogenous conformation of the protein. Antibodies generated in response to vaccination give a balanced Th1/Th2 response and target two previously discovered neutralizing epitopes.

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