Galactose/N-acetylgalactosamine lectin: The coordinator of host cell killing

Boettner, Douglas R.; Huston, Christopher D.; Petri, William A.

doi:10.1007/bf02704847

Cited by 13 publications

(11 citation statements)

References 44 publications

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“…Contact of the trophozoites via the Gal/GalNAc lectin triggers a signaling cascade initiating the death of the host cell through different mechanisms such as phagocytosis, cytotoxicity and caspase activation instigating the invasive (intestinal and/or extraintestinal) stages of the disease. Other molecules involved in the disease process include: a serine-rich E. histolytica protein (SREHP), amoebapores, and cysteine proteases (Boettner at al., 2002;. Activation of damaging inflammatory and non-inflammatory responses following contact of the trophozoites to the gut wall induces a massive neutrophil infiltration across the epithelium into the underlying tissues resulting in weakening of epithelial cells and the mucous layer and allowing trophozoites to invade the intestinal epithelium and disseminating to other bodily sites (Ackers and Mirelman, 2006).…”

Section: Intestinal Amoebiasismentioning

confidence: 99%

Amoebiasis in the Tropics: Epidemiology and Pathogenesis

Samie¹,

ElBakri²,

AbuOdeh³

2012

Current Topics in Tropical Medicine

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Section: Intestinal Amoebiasismentioning

confidence: 99%

Amoebiasis in the Tropics: Epidemiology and Pathogenesis

Samie¹,

ElBakri²,

AbuOdeh³

2012

Current Topics in Tropical Medicine

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“…Galactose/N-acetyl galactosamine-inhibitable lectin was reported to be responsible for the adherence of trophozoites to host cells, cytolysis, parasite invasion, and phagocytosis. [1][2][3] Cysteine proteases have been implicated in cytopathic activities such as damage of host cells and host tissue, induction of intestinal inflammation, and digestion of some components of the extracellular matrix. 4,5 Phagosomeassociated proteins such as EhRac A, EhPAK (p21-activated serine/threonine protein kinase), and actin have been reported to be involved in endocytosis and disease pathogenesis.…”

Section: Introductionmentioning

confidence: 99%

Entamoeba histolytica: Quantitative Proteomics Analysis Reveals Putative Virulence-Associated Differentially Abundant Membrane Proteins

Olivos-García

Lim

et al. 2018

The American Journal of Tropical Medicine and Hygiene

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Entamoeba histolytica is a protozoan parasite that causes amebiasis and poses a significant health risk for populations in endemic areas. The molecular mechanisms involved in the pathogenesis and regulation of the parasite are not well characterized. We aimed to identify and quantify the differentially abundant membrane proteins by comparing the membrane proteins of virulent and avirulent variants of E. histolytica HM-1:IMSS, and to investigate the potential associations among the differentially abundant membrane proteins. We performed quantitative proteomics analysis using isobaric tags for relative and absolute quantitation labeling, in combination with two mass spectrometry instruments, that is, nano-liquid chromatography (nanoLC)-matrix-assisted laser desorption/ionization-mass spectrometry/mass spectrometry and nanoLC-electrospray ionization tandem mass spectrometry. Overall, 37 membrane proteins were found to be differentially abundant, whereby 19 and 18 membrane proteins of the virulent variant of E. histolytica increased and decreased in abundance, respectively. Proteins that were differentially abundant include Rho family GTPase, calreticulin, a 70-kDa heat shock protein, and hypothetical proteins. Analysis by Protein ANalysis THrough Evolutionary Relationships database revealed that the differentially abundant membrane proteins were mainly involved in catalytic activities (29.7%) and metabolic processes (32.4%). Differentially abundant membrane proteins that were found to be involved mainly in the catalytic activities and the metabolic processes were highlighted together with their putative roles in relation to the virulence. Further investigations should be performed to elucidate the roles of these proteins in E. histolytica pathogenesis.Note: Supplemental information and figure appear at www.ajtmh.org.

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“…The ability of the parasite to cope up with increasing oxygen pressures and high concentration of reactive oxygen species (ROS) and reactive nitrogen species (RNS), contributes to its virulence (Stanley, Koester & Li, 1995) and a previous study has demonstrated the involvement of peroxiredoxin in this regard (Arias, 2012). Gal/GalNAc lectin is accountable for the virulence of E. histolytica and is reported to be involved in almost all the steps of pathogenesis (Boettner, 2002). Hence, it serves as a potential target for diagnosis and vaccination.…”

Section: Discussionmentioning

confidence: 99%

“…Gal/GalNAc lectin being a multimeric protein with a light subunit, heavy subunit and an intermediate subunit, surmounted the other two proteins in all aspects of antigenicity with 51 potent antigenic determinants within its sequence. Apart from its antigenic propensity, Gal/GalNAc lectin is structurally a highly conserved antigen (Boettner, 2002). Moreover, Gal/GalNAc lectin is a cell-wall protein that is easily accessible and recognized by the host immune system (Stanley, 1991;Boettner, 2002), thereby enhancing its antigenic profile.…”

Section: Discussionmentioning

confidence: 99%

“…Apart from its antigenic propensity, Gal/GalNAc lectin is structurally a highly conserved antigen (Boettner, 2002). Moreover, Gal/GalNAc lectin is a cell-wall protein that is easily accessible and recognized by the host immune system (Stanley, 1991;Boettner, 2002), thereby enhancing its antigenic profile. It mediates attachment of trophozoites to colonic mucins, increases parasite phospholipase A activity, maintains an acidic pH in amoebic intracellular vesicles and enhances cytolytic activity (Ravdin, 1989).…”

Section: Discussionmentioning

confidence: 99%

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Supplemental Information 1: Supplementary Files

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Background: Amoebiasis is the third most common parasitic cause of morbidity and mortality particularly in countries with poor hygienic settings. There exists an ambiguity in the diagnosis of amoebiasis, and hence arises a necessity for a better diagnostic approach. Serine-rich Entamoeba histolytica protein (SREHP), peroxiredoxin and Gal/GalNAc lectin are pivotal in E. histolytica virulence and are extensively studied as diagnostic and vaccine targets. For elucidating the cellular function of these proteins, details regarding their respective quaternary structures are essential which are not available till date. Hence, this study was carried out to predict the structure of these target proteins and characterize them structurally as well as functionally using relevant in-silico methods. Methods:The amino acid sequences of the proteins were retrieved from National Centre for Biotechnology Information database and aligned using ClustalW. Bioinformatic tools were employed in the secondary structure and tertiary structure prediction. The predicted structure was validated, and final refinement was carried out. Results: The protein structures predicted by i-TASSER were found to be more accurate than Phyre2 based on the validation using SAVES server. The prediction suggests SREHP to be a extracellular protein, peroxiredoxin was a peripheral membrane protein, while Gal/GalAc was found to be a cell-wall protein. Signal peptides were found in the amino-acid sequences of SREHP and Gal/GalNAc, whereas they were not present in the peroxiredoxin sequence. Gal/GalNAc lectin showed better antigenicity than the other two proteins studied. All three proteins exhibited similarity in their structures and were mostly composed of loops. Discussion:The structures of SREHP and peroxiredoxin were predicted successfully, while the structure of Gal/GalNAc lectin could not be predicted as it was a complex protein composed of three sub-units. Also, this protein showed less similarity with the available structural homologs. The quaternary structures predicted from this study would provide better structural and functional insights into these proteins and may aid in development of newer diagnostic assays or enhancement of the available treatment modalities.

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Galactose/N-acetylgalactosamine lectin: The coordinator of host cell killing

Cited by 13 publications

References 44 publications

Amoebiasis in the Tropics: Epidemiology and Pathogenesis

Amoebiasis in the Tropics: Epidemiology and Pathogenesis

Entamoeba histolytica: Quantitative Proteomics Analysis Reveals Putative Virulence-Associated Differentially Abundant Membrane Proteins

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