Abstract
Staphylococcus aureus is an opportunistic bacterial pathogen responsible for a diverse spectrum of human diseases and a leading cause of nosocomial and community-acquired infections. Development of a vaccine against this pathogen is an important goal. The fibronectin binding protein A (FnBPA) of S. aureus is one of multifunctional ‘microbial surface components recognizing adhesive matrix molecules' (MSCRAMMs). It is one of the most important adhesin molecules involved in the initial adhesion steps of S. aureus infection. It has been studied as potential vaccine candidates. However, FnBPA is a high-molecular-weight protein of 106 kDa and difficulties in achieving its high-level expression in vitro limit its vaccine application in S. aureus infection diseases control. Therefore, mapping the immunodominant regions of FnBPA is important for developing polyvalent subunit fusion vaccines against S. aureus infections. In the present study, we cloned and expressed the N-terminal and C-terminal of FnBPA. We evaluated the immunogenicity of the two sections of FnBPA and the protective efficacy of the two truncated fragments vaccines in a murine model of systemic S. aureus infection. The results showed recombinant truncated fragment F130-500 had a strong immunogenicity property and survival rates significantly increased in the group of mice immunized with F130-500 than the control group. We futher identified the immunodominant regions of FnBPA. The mouse antisera reactions suggest that the region covering residues 110 to 263 (F1B110-263) is highly immunogenic and is the immunodominant regions of FnBPA. Moreover, vaccination with F1B110-263 can generate partial protection against lethal challenge with two different S. aureus strains and reduced bacterial burdens against non-lethal challenge as well as that immunization with F130-500. This information will be important for further developing anti- S. aureus polyvalent subunit fusion vaccines.
Highlights
Staphylococcus aureus is an opportunistic bacterial pathogen responsible for a diverse spectrum of human diseases [1,2], which are from mild culture-confirmed skin and soft tissue infections to life-threatening and highly invasive disease [3,4,5]
The protein contains an N-terminal region that binds fibrinogen and elastin [21,22], and a C-terminal domain that interacts with fibronectin [23]. It is one of the most important adhesin molecules involved in the initial adhesion steps of S. aureus infection [24]
We evaluated the immunogenicity of the two sections of fibronectin binding protein A (FnBPA) by an enzymelinked immunosorbent assay (ELISA) and the protective efficacy of the two truncated fragments vaccines in a murine model of systemic S. aureus infection
Summary
Staphylococcus aureus is an opportunistic bacterial pathogen responsible for a diverse spectrum of human diseases [1,2], which are from mild culture-confirmed skin and soft tissue infections to life-threatening and highly invasive disease [3,4,5]. S. aureus possesses over 50 virulence factors [11], enabling the bacterium to adapt to a variety of host niches and to cause a multitude of diverse infections. These factors include a number of ‘microbial surface components recognizing adhesive matrix molecules’ (MSCRAMMs), capsular polysaccharides (CPs) and staphylococcal toxins [12,13,14]. MSCRAMMs are anchored to bacterial cell wall peptidoglycan by a mechanism that involves the enzyme sortase and a sorting signal that comprises a conserved
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