A proteomics analysis of the ovarian development in females of Haemaphysalis longicornis

  • Minjing Wang
  • Yuhong Hu
  • Mengxue Li
  • Qianqian Xu
  • Xiaoli Zhang
  • Xiaoshuang Wang
  • Xiaomin Xue
  • Qi Xiao
  • Jingze LiuEmail author
  • Hui WangEmail author


Haemaphysalis longicornis is an ixodid tick that can spread a wide variety of pathogens, affecting humans, livestock and wildlife health. The high reproductive capability of this species is initiated by the ingestion of a large amount of blood ingested by the engorged female tick. The degree of ovarian development is proportional to the number of eggs laid. Studying the regulatory mechanism of tick ovary development is relevant for the development of novel tick control methods. In this study, we used quantitative proteomics to study the dynamic changes in protein expression and protein phosphorylation during ovarian development of engorged female H. longicornis ticks. Synergistic action of many proteins (n = 3031) is required to achieve ovarian development and oocyte formation rapidly. Through bioinformatics analysis, changes in protein expressions and phosphorylation modifications in regulating the ovarian development of female ticks are described. Many proteins play an essential role during ovarian development. Also, protein phosphorylation appeared an important reproductive strategy to enable ticks to efficiently convert large amounts of blood in the ovaries into egg-producing components and ultimately produce many eggs.


Haemaphysalis longicornis Ovary Proteomics DIA Phosphorylation 



The authors are very grateful to Dr Baowen Zhang for her technical support in the use of mass spectrometer and helping in data analyse. This work was supported by the Natural Science Foundation for Excellent Youth Scholars of Hebei Province of China (No. C2017205135), the Natural Science Fund for Distinguished Young Scholars of Hebei Normal University (No. L2017J04).

Author contributions

HW designed experiments, analyzed the data, performed experiments, and wrote the initial manuscript. MW, YH, ML, XZ, performed experiments. XW, XX, QX prepared figures. JL designed experiments, correction of the manuscript.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

This study was approved by the Animal Ethics Committee of Hebei Normal University (Protocol Number: 165031) as complying with the animal protection law of the People’s Republic of China.

Supplementary material

10493_2020_469_MOESM1_ESM.jpg (322 kb)
Supplementary Figure S1. GO “Protein Class” analysis of differentially expressed 506 proteins and 545 phosphorylated proteins which were identified in ovary during all five stages of post-engorgement. a GO “Protein Class” analysis of differentially expressed proteins. b GO “Protein Class” analysis of all differentially expressed phosphorylated proteins (JPEG 322 kb)
10493_2020_469_MOESM2_ESM.jpg (339 kb)
Supplementary Figure S2. GO functional annotations for the differentially expressed proteins in the ovaries of female H. longicornis at five stages of post-engorgement (JPEG 339 kb)
10493_2020_469_MOESM3_ESM.jpg (375 kb)
Supplementary Figure S3. GO functional annotations for the differentially expressed phosphorylated proteins in the ovaries of female H. longicornis during five stages of post-engorgement (JPEG 375 kb)
10493_2020_469_MOESM4_ESM.jpg (390 kb)
Supplementary Figure S4. KEGG pathway analysis of the differentially expressed proteins in 4 Clusters. a-d KEGG pathway analysis of proteins in Cluster 1 to Cluster 4 (JPEG 390 kb)
10493_2020_469_MOESM5_ESM.xlsx (167 kb)
Supplementary Table S1. Statistics for protein quantification information of the common proteins were identified at five stages. These proteins were considered highly reliable, which at least 2 unique peptides were identified and have a CV < 20% among four replicates in each group (XLSX 167 kb)
10493_2020_469_MOESM6_ESM.xlsx (157 kb)
Supplementary Table S2. The data of phosphorylated peptides corresponding to differentially expressed phosphorylated proteins at five stages of post-engorgement. These phosphorylated peptides were considered highly reliable, which were have a CV < 20% among four replicates in each group (XLSX 156 kb)


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Copyright information

© Springer Nature Switzerland AG 2020

Authors and Affiliations

  • Minjing Wang
    • 1
  • Yuhong Hu
    • 2
  • Mengxue Li
    • 1
  • Qianqian Xu
    • 1
  • Xiaoli Zhang
    • 1
  • Xiaoshuang Wang
    • 1
  • Xiaomin Xue
    • 1
  • Qi Xiao
    • 1
  • Jingze Liu
    • 1
    • 3
    Email author
  • Hui Wang
    • 1
    • 3
    Email author
  1. 1.Hebei Key Laboratory of Animal Physiology, Biochemistry and Molecular Biology, College of Life SciencesHebei Normal UniversityShijiazhuangChina
  2. 2.Instrumental Analysis CenterHebei Normal UniversityShijiazhuangChina
  3. 3.ShijiazhuangChina

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