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ORIGINAL RESEARCH article

Front. Vet. Sci.
Sec. Parasitology
Volume 11 - 2024 | doi: 10.3389/fvets.2024.1387719
This article is part of the Research Topic Molecular, Multi-Omics and Computational Strategies for Effective Diagnosis and Control of Ticks and Tick-Borne Pathogens View all 4 articles

What are the main proteins in Haemaphysalis flava tick hemolymph?

Provisionally accepted
Dan Li Dan Li Lei Liu Lei Liu Zi-Ling Liu Zi-Ling Liu Yuan Tian Yuan Tian Xin Gao Xin Gao Tianyin Cheng Tianyin Cheng *
  • Hunan Agricultural University, Changsha, China

The final, formatted version of the article will be published soon.

    Background: Haemaphysalis flava is a notorious parasite for human and animals worldwide. The organs of H. flava are bathed in hemolymph which is a freely circulating fluid. The nutrients, immune factors and waste can be transported to every part of the body via hemolymph. The main soluble component in hemolymph are proteins. However, knowledge on the H. flava proteome is limited. Methods: Hemolymph was collected from fully engorged H. flava ticks by leg amputation. Hemolymph proteins were examined by both blue native polyacrylamide gel electrophoresis (BN-PAGE) and sodium dodecyl sulfate PAGE (SDS-PAGE). Proteins extracted from gels were further identified by a combination of liquid chromatography-tandem mass spectrometry (LC-MS/MS). Results: Two bands (380 kDa and 520 kDa) were separated from tick hemolymph by BN-PAGE and were further separated into four bands (105 kDa, 120 kDa, 130 kDa and 360 kDa) by SDS-PAGE. LC/MS/MS revealed that seven tick proteins and 13 host proteins existed in the four bands. These tick proteins mainly were the vitellogenin (Vg) family and αmacroglobulin family members. In silica structural analysis showed that these Vg family members all had common conserved domains including the N-terminus lipid binding domain (LPD-N), the C-terminus von Willebrand type D domain (vWD) and the unknown functional domain (DUF). Additionally, two of the Vg family proteins belonged to carrier protein (CP) by analyzing the unique N-terminal amino acid sequences and the cleaving sites. Conclusion: These findings imply that Vg family proteins and α-macroglobulin are the primary constituent of hemolymph in the form of protein complexes. Our results provide a valuable resource for further functional investigations of H. flava hemolymph effectors, and might be useful in tick management.

    Keywords: Haemaphysalis flava, Hemolymph, vitellogenin, Carrier protein, αmacroglobulin

    Received: 18 Feb 2024; Accepted: 19 Jun 2024.

    Copyright: © 2024 Li, Liu, Liu, Tian, Gao and Cheng. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Tianyin Cheng, Hunan Agricultural University, Changsha, China

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