# Antibody recognition of paramyxovirus surface proteins

> **NIH NIH R56** · FLORIDA STATE UNIVERSITY · 2024 · $682,008

## Abstract

While vaccines are available for SARS-CoV-2, influenza virus, and RSV, and our laboratory has advanced mAbs
and vaccines for hMPV, there has been a lack of research on parainfluenza virus (PIV) disease prevention and
treatment, despite being the second highest cause of acute lower respiratory infection (ALRI) in young children.
Globally, PIVs cause 18 million ALRI cases, 700,000 hospital admissions, and 34,000 deaths in children younger
than five years of age each year. As a comparison, RSV causes nearly 60,000 deaths in children under 5 years
of age each year, while hMPV causes approximately 12,000 deaths in the same age range. Among adults,
severe disease can occur in those with immuncompromising conditions, especially those with hematopoietic
stem cell and solid organ transplants, as well as those with hematologic malignancy, with high resulting mortality
rates. PIVs are members of the Paramyxoviridae family, which consists of both endemic viruses as well as
zoonotic viruses with pandemic potential. This R01 proposal seeks to advance the development of monoclonal
antibodies (mAbs) for the treatment of infectious diseases, which is a major priority of NIAID and our research
laboratory. Our major objective is to define the structural and mechanistic determinants mediating the
neutralization and protection against paramyxoviruses. For this proposal, we will specifically focus on the PIV
fusion (F) and hemagglutinin-neuraminidase (HN) surface proteins. In Aim 1, we will define the human B cell
repertoire to PIV HN and F in adults and children. We will leverage recent advances in single B cell sequencing
for the generation of human mAbs, which will then be assessed for neutralization potency, epitope specificity,
and interfering with the viral life cycle. In Aim 2, we will determine the optimal therapeutic strategy for anti-PIV
mAbs. We will utilize two rodent models, including Syrian golden hamsters for mAb screening, followed by cotton
rats for verification of therapeutic value. In Aim 3, we will determine the structural epitopes mediating antibody
functionality and protective efficacy. We will define these protective mAb epitopes at the molecular level using
cryo-electron microscopy, which will be essential to advancing the mAb candidates and future vaccine
candidates by identifying the optimal epitopes for mAb efficacy. With the recent approval of the first RSV vaccine,
and the critical use of antibody guided structure-based vaccine design to stabilize the RSV F protein in the pre-
fusion conformation, this proposal is conceptually innovative as we will incorporate recently described PIV pre-
fusion F proteins in our strategies, conduct the first in-depth B cell repertoire studies for PIV infection, and by the
exciting collaborations. Furthermore, this proposal is technically innovative as we will leverage state of the art
tools, including high-throughput single B cell sequencing and cryo-electron microscopy for determination of
protective and ...

## Key facts

- **NIH application ID:** 11131477
- **Project number:** 1R56AI181850-01
- **Recipient organization:** FLORIDA STATE UNIVERSITY
- **Principal Investigator:** Jarrod Mousa
- **Activity code:** R56 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $682,008
- **Award type:** 1
- **Project period:** 2024-08-16 → 2026-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/11131477

## Citation

> US National Institutes of Health, RePORTER application 11131477, Antibody recognition of paramyxovirus surface proteins (1R56AI181850-01). Retrieved via AI Analytics 2026-05-26 from https://api.ai-analytics.org/grant/nih/11131477. Licensed CC0.

---

*[NIH grants dataset](/datasets/nih-grants) · CC0 1.0*