Identification and initial characterization of matrix metalloproteinases in the yellow fever mosquito, Aedes aegypti

A. M. Kantor, S. Dong, N. L. Held, E. Ishimwe, A. L. Passarelli, R. J. Clem, A. W.E. Franz

Research output: Contribution to journalArticlepeer-review

Abstract

Aedes aegypti is a major vector for arboviruses such as dengue, chikungunya and Zika viruses. During acquisition of a viremic bloodmeal, an arbovirus infects mosquito midgut cells before disseminating to secondary tissues, including the salivary glands. Once virus is released into the salivary ducts it can be transmitted to another vertebrate host. The midgut is surrounded by a basal lamina (BL) in the extracellular matrix, consisting of a proteinaceous mesh composed of collagen IV and laminin. BL pore size exclusion limit prevents virions from passing through. Thus, the BL probably requires remodelling via enzymatic activity to enable efficient virus dissemination. Matrix metalloproteinases (MMPs) are extracellular endopeptidases that are involved in remodelling of the extracellular matrix. Here, we describe and characterize the nine Ae. aegypti encoded MMPs, AeMMPs 1−9, which share common features with other invertebrate and vertebrate MMPs. Expression profiling in Ae. aegypti revealed that Aemmp4 and Aemmp6 were upregulated during metamorphosis, whereas expression of Aemmp1 and Aemmp2 increased during bloodmeal digestion. Aemmp1 expression was also upregulated in the presence of a bloodmeal containing chikungunya virus. Using polyclonal antibodies, AeMMP1 and AeMMP2 were specifically detected in tissues associated with the mosquito midgut.

Original languageEnglish (US)
Pages (from-to)113-126
Number of pages14
JournalInsect molecular biology
Volume26
Issue number1
DOIs
StatePublished - Feb 1 2017

Keywords

  • Aedes aegypti
  • basal lamina
  • bloodmeal
  • catalytic domain
  • matrix metalloproteinase
  • midgut
  • phylogeny
  • virus dissemination

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Insect Science

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