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Review
. 2024 Aug;151(9):1063-1073.
doi: 10.1017/S0031182024001410.

Glycine rich proteins of ticks: more than a cement component

Affiliations
Review

Glycine rich proteins of ticks: more than a cement component

Renata Perotto de Souza et al. Parasitology. 2024 Aug.

Abstract

Glycine-rich proteins (GRPs) are arbitrarily defined as those containing 20% or more glycine residues and constitute a superfamily divided into subfamilies based on their structure and/or function. GRPs have been identified in a diverse array of organisms and have been shown to possess a number of distinctive biological characteristics, including nucleic acid binding, adhesive glue-like properties, antimicrobial activity, involvement in the stress response and in the formation of cuticle components. In ticks, their expression has been described and studied mainly in the salivary glands, and their primary function is usually associated with cement formation and/or structure. Conversely, several GRPs are present in all tick developmental stages, and the expression of many GRP genes is modulated by physiological processes and immune challenges, such as feeding and pathogen infection. Considering that some tick GRPs appear to play essential roles in the tick life cycle, they have been evaluated as immune targets, with a focus on their potential application in vaccine development. This review highlights the roles that tick GRPs may perform beyond the formation and maintenance of the cement scaffold, including structural characterization, locations and functional relevance, hypothetical functions, and their potential use in anti-tick vaccine development.

Keywords: Tick salivary proteins; tick-host relationship; vaccine.

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Conflict of interest statement

The authors declare no conflicts of interest exist.

Figures

None
Graphical abstract
Figure 1.
Figure 1.
Gly-repeat patterns in tick GRP sequences. Each repeat is represented with a different color, and pattern variations within sequences are highlighted with the respective color. Sequences presented are: 64P of Haemaphysalis longicornis (AAM09648.1), RmGRP of Rhipicephalus microplus (AQX36208.1), Sal 1 of Rhipicephalus annulatus (AGR45924.1), NPL-2 of Ixodes scapularis (EEC15723.1), Ctenidin-1-like of Ixodes scapularis (XP_029830867.1), and Aam-3099 of Amblyomma americanum (JAG92486.1).

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