Identification and characterization of the fibrinogen-like domain of fibrinogen-related proteins in the mosquito, Anopheles gambiae, and the fruitfly, Drosophila melanogaster, genomes

Xinguo Wang,Qin Zhao,Bruce M Christensen

doi:10.1186/1471-2164-6-114

Xinguo Wang, Qin Zhao + Show 1 more

Open Access

https://doi.org/10.1186/1471-2164-6-114

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Abstract

BackgroundThe fibrinogen-like (FBG) domain, which consists of approximately 200 amino acid residues, has high sequence similarity to the C-terminal halves of fibrinogen β and γ chains. Fibrinogen-related proteins (FREPs), which contain FBG domains in their C-terminal region, are found universally in vertebrates and invertebrates. In invertebrates, FREPs are involved in immune responses and other aspects of physiology. To understand the complexity of this family in insects, we analyzed FREPs in the mosquito genome and made comparisons to FREPs in the fruitfly genome.ResultsBy using the genome data of the mosquito, Anopheles gambiae, 53 FREPs were identified, whereas only 20 members were found in the Drosophila melanogaster genome. Using sequence profile analysis, we found that FBG domains have high sequence similarity and are highly conserved throughout the FBG domain region. By secondary structure analysis and comparison, the FBG domains of FREPs are predicted to function in recognition of carbohydrates and their derivatives on the surface of microorganisms in innate immunity.ConclusionDetailed sequence and structural analysis discloses that the FREP family contains FBG domains that have high sequence similarity in the A. gambiae genome. Expansion of the FREP family in mosquitoes during evolutionary history is mainly accounted for by a major expansion of the FBG domain architecture. The characterization of the FBG domains in the FREP family is likely to aid in the experimental analysis of the ability of mosquitoes to recognize parasites in innate immunity and physiologies associated with blood feeding.

Highlights

The fibrinogen-like (FBG) domain, which consists of approximately 200 amino acid residues, has high sequence similarity to the C-terminal halves of fibrinogen β and γ chains
Identification of fibrinogen-related proteins (FREP) genes and characterization of the FBG domain in the A. gambiae genome To identify FREP proteins encoded in the A. gambiae genome, a PSI-basic local alignment search tool (BLAST) search was performed using AL-1 as a query sequence to screen the A. gambiae genome database at National Center for Biotechnology Information (NCBI)
To find FREPs that may have been overlooked due to low sequence identity to AL-1, we selected each sequence from the search results as a new seed to search the A. gambiae genome database again

Summary

Introduction

The fibrinogen-like (FBG) domain, which consists of approximately 200 amino acid residues, has high sequence similarity to the C-terminal halves of fibrinogen β and γ chains. Three distinct fibrinogen-related proteins (FREPs) have been identified in human: ficolin, tenascins, and microfibril-associated protein (MAP) [3,4,5]. These (page number not for citation purposes). Tenascins are a family of multifunctional extracellular matrix (ECM) glycoproteins subject to complex spatial and temporal patterns of expression in the course of various organogenetic processes. These proteins mediate cell adhesion and show tissue-specific and cell growth-associated expression [4]. Microfibril-associated protein, another extracellular matrix protein, is a component of connective tissue microfibrils and a candidate for involvement in the etiology of inherited connective tissue diseases, which are associated with the Smith-magenis syndrome, a multiple congenital anomaly/mental retardation syndrome [8]

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