In silico screening and immunogenic features of putative tick cement protein PA107 from Ixodes ricinus tick.

Exp Appl Acarol

Group for Medical Entomology, Centre of Excellence for Food- and Vector-Borne Zoonoses, Institute for Medical Research, National Institute of Republic of Serbia, University of Belgrade, Belgrade, Serbia.

Published: January 2025

Tick salivary proteins are crucial for efficient and successful tick feeding. Most of them are still uncharacterized, especially those involved in the formation of tick cement. Tick salivary protein PA107 is a putative cement protein, which is transcribed in salivary glands during the initial phase of tick feeding. It is a tick-unique protein, with homologs described in several tick genera. In this study, a detailed in silico analysis of its primary and tertiary structure was performed, along with the immunogenicity assessment for the PA107 protein from Ixodes ricinus species. The screening of the primary structure placed it to the glycine-rich protein family, revealing in parallel an overlapping 15mer at the C-terminus and borderline homology to non-tick proteins with antimicrobial activity. The analysis of tertiary structure revealed a high degree of intrinsic disorder for monomeric PA107, in contrast to highly ordered structures for different oligomeric states that might correlate with the putative role in the tick cement formation process. Regarding in silico PA107 immunogenicity inference, obtained results were inconclusive, which aligns with the in vitro findings showing definitely the lack of humoral response induction in experimentally infested rats and persons bitten by the I. ricinus ticks. The results represent new pieces of a huge puzzle depicting a complex tick-host relationship, but also identify PA107 as a possible compound of novel formulations to be used in biomedicine as bioadhesives, and as a target for new anti-tick strategies, by interfering with the cement cone formation and stability, i.e. tick attachment and feeding.

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Source
http://dx.doi.org/10.1007/s10493-025-01001-1DOI Listing

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