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Lee, Young Ah,Saito-Nakano, Yumiko,Kim, Kyeong Ah,Min, Arim,Nozaki, Tomoyoshi,Shin, Myeong Heon Elsevier 2015 Experimental parasitology Vol.149 No.-
<P><B>Abstract</B></P> <P> <I>Entamoeba histolytica</I> is an enteric tissue-invading protozoan parasite that causes amoebic colitis and occasionally liver abscess in humans. During tissue invasion, amoebic adhesion to host components is an important event for host cell death leading to successful invasion and infection. Among amoebic virulence factors, Gal/GalNAc lectin is known to be major adhesion factor to host cells. In this study, we investigated the role of amoebic secreted CP (Cysteine Proteases) in amoebic adhesion to extracellular matrix (ECM) protein using CP inhibitor and <I>E.?histolytica</I> strains in which the endogenous inhibitor of cysteine protease (ICP) 1 gene was overexpressed (ICP1<SUP>+</SUP>) or repressed by antisense small RNA-mediated gene silencing (ICP1<SUP>−</SUP>). We found that pretreatment of wild-type amoebae with CP inhibitor E64, or thiol-group modifiers such as diamide and <I>N</I>-Ethylmaleimide resulted in a significant decrease in adhesion to laminin and collagen ECM proteins. Furthermore, ICP1<SUP>+</SUP> strain, with a reduction of secreted CP activity, exhibited reduced ability by 40% to adhere to laminin. In contrast, ICP1<SUP>−</SUP> strain, with a 1.9-fold increase of secreted CP activity, showed a two-fold increase in amoebic adherence to laminin compared to the control strain. In addition, total amount of secreted CP5 was decreased in ICP1<SUP>+</SUP> amoeba. Conversely, total amount of secreted CP1 and mature-form CP5 were increased in ICP1<SUP>−</SUP> amoeba. We also found that ICP1 was secreted into extracellular milieu. These results suggest that secreted CP activity by <I>E.?histolytica</I> may be an important factor affecting adhesion to host proteins, and regulation of CP secretion by ICP plays a major role in pathogenesis. This study provides insight into the CP-mediated tissue pathogenesis in amoeba-invaded lesions during human amoebiasis.</P> <P><B>Highlights</B></P> <P> <UL> <LI> <I>Entamoeba histolytica</I> has the endogenous cysteine protease inhibitor (ICP) 1 gene. </LI> <LI> Modulation of CP activity alters <I>E.?histolytica</I> adhesion to ECM proteins. </LI> <LI> Pretreated amoebae with E64 significantly decrease adhesion to ECM proteins. </LI> <LI> ICP1<SUP>+</SUP> strain exhibited reduced ability by 40% to adhere to laminin. </LI> <LI> Adherence of ICP1<SUP>−</SUP> strain increased two-fold compared to the control strain. </LI> </UL> </P>
Sanjib Kumar Sardar,Ajanta Ghosal,Yumiko Saito-Nakano,Shanta Dutta,Tomoyoshi Nozaki,Sandipan Ganguly 대한기생충학열대의학회 2021 The Korean Journal of Parasitology Vol.59 No.4
In this study, we have collected and screened a total of 268 stool samples from diarrheal patients admitted to an Infectious disease hospital in Kolkata for the presence of Cryptosporidium spp. The initial diagnosis was carried out by microscopy followed by genus specific polymerase chain reaction assays based on 70 kDa heat shock proteins (HSP70). DNA sequencing of the amplified locus has been employed for determination of genetic diversity of the local isolates. Out of 268 collected samples, 12 (4.48%) were positive for Cryptosporidium spp. Sequences analysis of 70 kDa heat shock proteins locus in 12 Cryptosporidium local isolates revealed that 2.24% and 1.86% of samples were showing 99% to 100% identity with C. parvum and C. hominis. Along with the other 2 major species one recently described globally dis-tributed pathogenic species Cryptosporidium viatorum has been identified. The HSP70 locus sequence of the isolate showed 100% similarity with a previously described isolate of C. viatorum (Accession No. JX978274.1, JX978273.1, and JN846706.1) present in GenBank.