Regular ArticlePartial Characterization of the Proteolytic Secretions of Acanthamoeba polyphaga
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Acanthamoeba mauritaniensis genotype T4D: An environmental isolate displays pathogenic behavior
2020, Parasitology InternationalCitation Excerpt :Supernatants were collected, and their absorbances were read with a spectrophotometer at 520 nm to determine the Azocoll activities as reported by Serrano-Luna et al, (2006) [25]. Protease activities were reported as milliunits per milligram; this unit of measure is equivalent to the amount of substrate degraded in 1 min per milligram of TCE or per milliliter of CM [9]. TCE and CM were preincubated with protease inhibitors (at the concentrations described above) at room temperature for 1 h before incubation with the substrate.
Neoparamoeba perurans loses virulence during clonal culture
2015, International Journal for ParasitologyIn vitro inhibition of protease-activated receptors 1, 2 and 4 demonstrates that these receptors are not involved in an Acanthamoeba castellanii keratitis isolate-mediated disruption of the human brain microvascular endothelial cells
2014, Experimental ParasitologyCitation Excerpt :Previous studies have identified a number of factors associated with Acanthamoeba pathogenesis. These include adhesins, i.e., mannose-binding protein (Garate et al., 2004), laminin-binding protein (Hong et al., 2004), phospholipases (Mortazavi et al., 2011; Matin and Jung, 2011), and extracellular proteases, including serine (Na et al., 2001; Mitro et al., 1994; Leher et al., 1998; Khan et al., 2000), cysteine (Hadas and Mazur, 1993) and metalloproteases (Alsam et al., 2005; Sissons et al., 2006; Siddiqui and Khan, 2012). Among extracellular proteases, recent studies showed that serine proteases play a key role in amoebae traversal of the blood–brain barrier, a key step in the development of amoebic encephalitis (Edwards-Smallbone et al., 2012; Khan and Siddiqui, 2009).
Area 51: How do Acanthamoeba invade the central nervous system?
2011, Trends in ParasitologyCitation Excerpt :These findings were supported using the serine protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), which abolished protease-mediated human brain microvascular endothelial cells (HBMEC) permeability and loss of transendothelial electrical resistance [7]. Several extracellular serine proteases have been identified with approximate molecular weights ranging from 12 to 230 kDa [26–33]. Of these, the 133 kDa serine protease MIP133 is identified as a crucial component of the pathogenic cascade of Acanthamoeba.
Acanthamoeba castellanii: Morphological analysis of the interaction with human cornea
2010, Experimental ParasitologyElastase secretion in Acanthamoeba polyphaga
2009, Acta TropicaCitation Excerpt :Tissue damage and invasion then proceed through phagocytic activity and cytopathic effects by molecules released by the parasites; among them are proteolytic enzymes (Alizadeh et al., 1994; Mattana et al., 2002; Marciano-Cabral and Cabral, 2003; Alsam et al., 2005; Clarke and Niederkorn, 2006). In addition to studies demonstrating that secretion of certain serine and metallopeptidases can be induced by trophozoite–host cell contact or addition of mannose to the culture medium (Cao et al., 1998; Leher et al., 1998; Hurt et al., 2003), Acanthamoeba spp. constitutively secrete appreciable amounts of serine and cysteine peptidases (He et al., 1990; Mitro et al., 1994; Mitra et al., 1995; Alfieri et al., 2000; Kong et al., 2000; Cho et al., 2000; Na et al., 2001; Sissons et al., 2006). Constitutive secretion of metallopeptidases has also been demonstrated in A. castellanii (Alsam et al., 2005; Sissons et al., 2006), and suggested in Acanthamoeba polyphaga (Mitro et al., 1994; Alfieri et al., 2000).