Host-derived transferrin is maintained and transferred from midgut to ovary in Haemaphysalis longicornis ticks

Ticks Tick Borne Dis. 2014 Mar;5(2):121-6. doi: 10.1016/j.ttbdis.2013.09.004. Epub 2013 Nov 20.

Abstract

Transferrin is known to be an iron transporter in vertebrates and several arthropods. Iron from host blood is essential for ovarian development in blood-sucking arthropods. However, tick transferrin has been identified in only a few species, and its function has yet to be elucidated, resulting in incomplete understanding of iron metabolism in ticks. Here, we investigated the transfer of host-derived transferrin in the hard tick Haemaphysalis longicornis using immunological methods. Western blot showed that host-derived transferrin was maintained in all developmental stages of ticks up to 28 days after engorgement and was detected in the midgut and the ovary of adult females following blood feeding. However, no host-derived transferrin was detected in eggs after laying or in larvae after hatching, indicating that host-derived transferrin is not transferred to offspring transovarially. Indirect immunofluorescent antibody testing showed the localization of host-derived transferrin in digestive cells of the midgut and oocytes of the ovary from engorged adult females. These results suggest that host-derived transferrin is transferred to the ovary through the midgut and the hemolymph, and raise the possibility of the function of host-derived transferrin as an iron source in the ovary, providing additional insight on iron metabolism in ticks.

Keywords: Haemaphysalis longicornis; Iron; Iron-binding protein; Protein transfer; Transferrin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies / immunology
  • Antibody Specificity
  • Feeding Behavior
  • Female
  • Gastrointestinal Tract / metabolism*
  • Ixodidae / growth & development
  • Ixodidae / metabolism*
  • Ovary / metabolism*
  • Rabbits
  • Transferrin / metabolism*

Substances

  • Antibodies
  • Transferrin