Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2008 Mar;54(3):573-85.
doi: 10.1016/j.jinsphys.2007.12.006. Epub 2007 Dec 23.

HlLgm2, a member of asparaginyl endopeptidases/legumains in the midgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion

M Abdul Alim  1 , Naotoshi Tsuji, Takeharu Miyoshi, M Khyrul Islam, Xiaohong Huang, Takeshi Hatta, Kozo Fujisaki
Affiliations

HlLgm2, a member of asparaginyl endopeptidases/legumains in the midgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion

M Abdul Alim et al. J Insect Physiol. 2008 Mar.

Abstract

Here we describe a cDNA encoding the second asparaginyl endopeptidase/legumain (HlLgm2) from the midgut of the ixodid tick Haemaphysalis longicornis. Endogenous HlLgm2 was expressed in all the developmental stages of the tick, localized mainly in the midgut epithelium and was up-regulated by the host blood-feeding process, as demonstrated by immunoblotting and immunohistochemistry. RT-PCR and real-time PCR showed that the HlLgm2 gene was expressed at a lower level during all phases of blood-feeding than our previously characterized legumain (HlLgm) gene from the same tick. More strikingly, there was no expression of HlLgm2 mRNA beyond 96 h of blood-feeding, while HlLgm mRNA expression continued until full engorgement. Escherichia coli-expressed recombinant HlLgm2 (rHlLgm2) efficiently hydrolysed the legumain-specific synthetic substrate. rHlLgm2 activity was inhibited by iodoacetamide and N-ethylmaleimide and also by Fe(2+), Cu(2+), Co(2+) and Ni(2+). rHlLgm2 digested bovine haemoglobin and exhibited strict specificity for the asparaginyl bonds on the carboxy-terminal side of a peptide, as demonstrated by internal amino acid sequence analysis of the cleaved bovine serum albumin products. Our results suggest that HlLgm2, together with HlLgm, plays a pivotal role in host blood-meal digestion process.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

Publication types

LinkOut - more resources