Abstract
Tetraspanins are membrane proteins involved in intra- and/or intercellular signaling, and membrane protein complex formation. In some organisms, their role is associated with virulence and pathogenesis. Here, we investigate known and potential tetraspanins in the human intestinal protozoan parasite Entamoeba histolytica. We conducted sequence similarity searches against the proteome data of E. histolytica and newly identified nine uncharacterized proteins as potential tetraspanins in E. histolytica. We found three subgroups within known and potential tetraspanins, as well as subgroup-associated features in both their amino acid and nucleotide sequences. We also examined the subcellular localization of a few representative tetraspanins that might be potentially related to pathogenicity. The results in this study could be useful resources for further understanding and downstream analyses of tetraspanins in Entamoeba.
Highlights
The human intestinal parasite, Entamoeba histolytica, is a pathogen that causes amoebiasis
Nucleotide sequences, including introns, of tetraspanin genes in E. histolytica and in four other Entamoeba species (i.e., E. dispar, E. invadens, E. moshkovskii and E. nuttalli) and amino acid sequences of tetraspanins in other Entamoeba were retrieved from AmoebaDB (41 Released) [21]
One of the proteins used in the former study [19], EAL45935 (EHI_139370; UniProtKB AC: C4M6W3) is a high mobility group (HMG) box domain containing protein, according to the annotation provided by UniProt, and contains only a single cysteine residue
Summary
The human intestinal parasite, Entamoeba histolytica, is a pathogen that causes amoebiasis. This disease is characterized by colitis, often manifested by symptoms such as diarrhea and dysentery. It affects millions worldwide and causes up to 73,800 deaths annually [1]. Extraintestinal complications of amoebiasis arise when the parasite establishes colonization of other organs such as the liver, leading to amoebic liver abscess formation. The virulence of this parasite is due to its ability to inflict damage to host cells and tissues, which involve processes that are directly caused or regulated by membrane proteins. Among them are the galactose and N-acetyl-d-galactosamine specific lectin [2], adhesin [3], and the lysine and glutamic acid enriched protein (KERP1) [4], involved in parasite attachment to colonic epithelial cells, and rhomboid protease [5], which contribute to immune evasion
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
