Phylogenetic study and comparison of different TbpB obtained from Glaesserella parasuis present in Spanish clinical isolates.

Abstract

Glaesserella parasuis (Gp) is the etiological agent of Glässer's disease (GD), which causes important economic losses for the pig intensive production worldwide. This organism uses a smart protein-based receptor to acquire specifically iron from the porcine transferrin. This surface receptor consists of transferrin-binding protein A (TbpA) and transferrin-binding protein B (TbpB). TbpB has been considered the most promising antigen to formulate a based-protein vaccine with broad-spectrum of protection against GD. The purpose of our study was to determine the capsular diversity of Gp clinical isolates collected in different Spanish regions between 2018 and 2021. A total of 68 Gp isolates were recovered from porcine respiratory or systemic samples. A species-specific PCR based on tbpA gene, followed by multiplex PCR for typing Gp isolates were performed. Serovars 5, 10, 2, 4 and 1 were the most prevalent and involved almost 84% of isolates. TbpB amino acid sequences from 59 of these isolates were analyzed, and a total of ten clades could be established. All of them showed a wide diversity with respect to capsular type, anatomical isolation site and geographical origin, with minor exceptions. Regardless of the serovars, the in silico analysis of TbpB sequences revealed that a vaccine based on a TbpB recombinant protein could potentially prevent Glässer's disease outbreaks in Spain.