Abstract

BackgroundAquaporins (AQPs) and aquaglyceroporins (AQGPs) belong to the superfamily of Major Intrinsic Proteins (MIPs) and are involved in the transport of water and neutral solutes across the membranes. MIP channels play significant role in plant-fungi symbiotic relationship and are believed to be important in host-pathogen interactions in human fungal diseases. In plants, at least five major MIP subfamilies have been identified. Fungal MIP subfamilies include orthodox aquaporins and five subgroups within aquaglyceroporins. XIP subfamily is common to both plants and fungi. In this study, we have investigated the extent of diversity in fungal MIPs and explored further evolutionary relationships with the plant MIP counterparts.ResultsWe have extensively analyzed the available fungal genomes and examined nearly 400 fungal MIPs. Phylogenetic analysis and homology modeling exhibit the existence of a new MIP cluster distinct from any of the known fungal MIP subfamilies. All members of this cluster are found in microsporidia which are unicellular fungal parasites. Members of this family are small in size, charged and have hydrophobic residues in the aromatic/arginine selectivity filter and these features are shared by small and basic intrinsic proteins (SIPs), one of the plant MIP subfamilies. We have also found two new subfamilies (δ and γ2) within the AQGP group. Fungal AQGPs are the most diverse and possess the largest number of subgroups. We have also identified distinguishing features in loops E and D in the newly identified subfamilies indicating their possible role in channel transport and gating.ConclusionsFungal SIP-like MIP family is distinct from any of the known fungal MIP families including orthodox aquaporins and aquaglyceroporins. After XIPs, this is the second MIP subfamily from fungi that may have possible evolutionary link with a plant MIP subfamily. AQGPs in fungi are more diverse and possess the largest number of subgroups. The aromatic/arginine selectivity filter of SIP-like fungal MIPs and the δ AQGPs are unique, hydrophobic in nature and are likely to transport novel hydrophobic solutes. They can be attractive targets for developing anti-fungal drugs. The evolutionary pattern shared with their plant counterparts indicates possible involvement of new fungal MIPs in plant-fungi symbiosis and host-pathogen interactions.

Highlights

  • Aquaporins (AQPs) and aquaglyceroporins (AQGPs) belong to the superfamily of Major Intrinsic Proteins (MIPs) and are involved in the transport of water and neutral solutes across the membranes

  • Identification of fungal MIPs and their taxonomic distributions Ten MIP sequences representing different subfamilies and organism groups were used as query sequences in the PSI-BLAST and BLAST searches to search the nonredundant database in NCBI and UniProt database [52] respectively

  • The MIP sequences are diverse, they all adopt a characteristic hour-glass helical fold consisting of six transmembrane helical segments (TM1 to TM6) and two functionally important loops with half-helices (LB and LE) which meet in the middle of the membrane (Figure 1)

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Summary

Introduction

Aquaporins (AQPs) and aquaglyceroporins (AQGPs) belong to the superfamily of Major Intrinsic Proteins (MIPs) and are involved in the transport of water and neutral solutes across the membranes. MIP channels play significant role in plant-fungi symbiotic relationship and are believed to be important in host-pathogen interactions in human fungal diseases. The superfamily of Major Intrinsic Proteins (MIPs) contains channel proteins that transport water and other neutral solutes [1,2,3,4] These integral membrane proteins are found from bacteria to humans and are abundantly present in plants [5,6]. MIP members play significant role in kidney nephron, epithelial fluid secretion, maintaining brain water balance, cell migration, skin hydration, adipocyte metabolism and neuroexcitation [9,13,14,15]. We have recently identified more than 1000 MIP genes from more than 340 organisms and details about the genes, protein products and structural models are available in MIPModDB database [6]

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