Decoration of Burkholderia Hcp1 protein to virus-like particles as a vaccine delivery platform

Author:

Khakhum Nittaya1,Baruch-Torres Noe2,Stockton Jacob L.1,Chapartegui-González Itziar1ORCID,Badten Alexander J.13,Adam Awadalkareem1,Wang Tian1,Huerta-Saquero Alejandro14ORCID,Yin Y. Whitney2,Torres Alfredo G.15ORCID

Affiliation:

1. Department of Microbiology & Immunology, University of Texas Medical Branch, Galveston, Texas, USA

2. Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, Galveston, Texas, USA

3. Institute for Translational Sciences, Galveston, Texas, USA

4. Centro de Nanociencias y Nanotecnología, Universidad Nacional Autónoma de México, Ensenada, Baja California, Mexico

5. Department of Pathology, University of Texas Medical Branch, Galveston, Texas, USA

Abstract

ABSTRACT Virus-like particles (VLPs) are protein-based nanoparticles frequently used as carriers in conjugate vaccine platforms. VLPs have been used to display foreign antigens for vaccination and to deliver immunotherapy against diseases. Hemolysin-coregulated proteins 1 (Hcp1) is a protein component of the Burkholderia type 6 secretion system, which participates in intracellular invasion and dissemination. This protein has been reported as a protective antigen and is used in multiple vaccine candidates with various platforms against melioidosis, a severe infectious disease caused by the intracellular pathogen Burkholderia pseudomallei . In this study, we used P22 VLPs as a surface platform for decoration with Hcp1 using chemical conjugation. C57BL/6 mice were intranasally immunized with three doses of either PBS, VLPs, or conjugated Hcp1-VLPs. Immunization with Hcp1-VLPs formulation induced Hcp1-specific IgG, IgG 1 , IgG 2c , and IgA antibody responses. Furthermore, the serum from Hcp1-VLPs immunized mice enhanced the bacterial uptake and opsonophagocytosis by macrophages in the presence of complement. This study demonstrated an alternative strategy to develop a VLPs-based vaccine platform against Burkholderia species.

Publisher

American Society for Microbiology

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