Disease relevance of espP

• Functional analysis showed that EspP is a protease capable of cleaving pepsin A and human coagulation factor V. Degradation of factor V could contribute to the mucosal haemorrhage observed in patients with haemorrhagic colitis [1].
• The deduced amino acid sequence of EspP showed homology to several secreted or surface-exposed proteins of pathogenic bacteria, in particular EspC of enteropathogenic E. coli and IgA1 proteases from Neisseria spp. and Haemophilus influenzae [1].
• Examination of 201 diarrhoeagenic E. coli strains using a newly developed espP-specific PCR showed that espP is specific for STEC and present in 57% of STEC belonging to 16 different serotypes [2].
• Other plasmidborne virulence factors, such as ehxA, katP, and espP, were acquired later by the enterohemorrhagic E. coli 1 complex in a stepwise manner [3].
• Here we characterize this region in EspP, a prototype of the serine protease autotransporters of enterobacteriaceae [4].

High impact information on espP

• Remarkably, modification of the signal peptide caused EspP to misfold in the periplasm and blocked transport of the passenger domain across the outer membrane [5].
• The corresponding espP gene consists of a 3900 bp open reading frame that is able to encode a 1300-amino-acid protein [1].
• Among the plasmid-borne determinants, E-hly and espP were the most common and E-hly might be a pathogenicity marker among EHEC non-O157 strains [6].
• The espP genes of the 16 STEC serotypes varied to a certain extent, as shown by nucleotide sequence and restriction enzyme analyses, but the DNA regions adjacent to the espP gene were completely different [2].
• The aim of this study was to investigate, using the example of the plasmid-encoded serine protease EspP, whether these plasmids are a uniform genetic element present in STEC [2].

Chemical compound and disease context of espP

• All strains of O157 had the genes coding for verocytotoxin (VT) 2, intimin (eaeA), E. coli hemolysin (E-hly), and secreted serine protease (espP) [6].

Biological context of espP

• In the most prevalent STEC serogroup, O157, it was observed that the plasmid of sorbitol-fermenting STEC O157:H- lacks the espP and katP genes although both genes are present in the plasmid of the non-sorbitol-fermenting STEC O157:H7 [2].

Analytical, diagnostic and therapeutic context of espP

• A comparison of 77 isolates of bovine origin and 91 human isolates belonging to six major serotypes showed significant associations of the genes for Shiga toxin 1 and EspP protease with bovine isolates and an increased adherence on HEp-2 cell cultures for human isolates, particularly from diarrheic patients and healthy persons [7].

References