Disease relevance of yscD

• In Yersinia pestis KIM, there are 11 Yops (yersinial outer membrane proteins) encoded by the low-Ca2+ response virulence plasmid pCD1 [1].
• Evading TLR4 activation by lipid A alteration may contribute to the virulence of various Gram-negative bacteria [2].
• TcpP protein is a positive regulator of virulence gene expression in Vibrio cholerae [3].
• HecA, a member of a class of adhesins produced by diverse pathogenic bacteria, contributes to the attachment, aggregation, epidermal cell killing, and virulence phenotypes of Erwinia chrysanthemi EC16 on Nicotiana clevelandii seedlings [4].
• Strikingly, an orthologous HPI is a widely distributed virulence determinant among Escherichia coli and other Enterobacteriaceae which cause extraintestinal infections [5].

Psychiatry related information on yscD

• This comparative proteomic characterization of host response clearly shows that host protein expression patterns are distinct for the different pathogen exposures, and contributes to further understanding of Y. pestis virulence and host defense mechanisms [6].

High impact information on yscD

• Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection [7].
• Using this mutant organism as a relevant biological probe, we demonstrate here that the calcium concentration in Y. pestis-containing phagolysosomes is sufficiently low to permit virulence gene expression; this resolves the question of where Y. pestis might express its Ca2+-regulated genes in vivo [8].
• Moreover, cloned pla was sufficient to restore segregants lacking the entire pla-bearing plasmid to full virulence [9].
• The virulence plasmid contains some evolutionary remnants including, in Y. enterocolitica, an operon encoding resistance to arsenic compounds [10].
• The virulence plasmid of Yersinia, an antihost genome [10].

Chemical compound and disease context of yscD

• Yersiniabactin (Ybt) synthetase is a three-subunit, 17-domain [7 domains in high molecular weight protein (HMWP)2, 9 in HMWP1, and 1 in YbtE] enzyme producing the virulence-conferring siderophore yersiniabactin in Yersinia pestis [11].
• The Yfe system of Yersinia pestis transports iron and manganese and is required for full virulence of plague [12].
• Structural organization of the pFra virulence-associated plasmid of rhamnose-positive Yersinia pestis [13].
• The independent abilities of Yersinia pestis to absorb exogenous pigments including hemin and Congo red (Pgm+) and to produce the bacteriocin pesticin with genetically linked invasive enzymes (Pst+) are established virulence factors of the species [14].
• The causative agent of plague, Yersinia pestis, contains a 75-kb plasmid, pCD1, which carries a virulence-related stimulon called the low-Ca2+ response stimulon (LCRS) [15].

Biological context of yscD

• The complete nucleotide sequence and gene organization of the three virulence plasmids from Yersinia pestis KIM5 were determined [16].
• Plasmid pPCP1 (9,610 bp) has a GC content of 45.3% and encodes two previously known virulence factors, an associated protein, and a single copy of IS100 [16].
• Strains often differ in their ability to cause disease, and comparative genomics is uncovering novel virulence determinants, hidden aspects of pathogenesis, and new targets for vaccine development [17].
• Yersinia pestis, the plague bacillus, has an exceptional pathogenicity but the factors responsible for its extreme virulence are still unknown [18].
• Apparently, the expression of the O-antigen is not beneficial for the virulence or to the lifestyle of Y. pestis and, therefore, as one step in the evolution of Y. pestis, the O-antigen gene cluster was inactivated [19].

Anatomical context of yscD

• Y. pestis possesses three plasmids, of which one, shared by the enteropathogenic species, mediates a number of virulence factors that directly or indirectly promote survival within macrophages and immunosuppression [20].
• A 70-kb virulence plasmid (sometimes called pYV) enables Yersinia spp. to survive and multiply in the lymphoid tissues of their host [21].
• The activation response of neutrophils to nonpathogenic bacteria is greatly altered by exposure to Yersinia pestis, which may be a major factor contributing to the virulence and rapid progression of plague [22].
• Activation of bacterial virulence-associated type III secretion systems (T3SSs) requires direct contact between a bacterium and a eukaryotic cell [23].
• These data indicate that the YscF needle is a multifunctional structure that participates in virulence protein secretion, in translocation of virulence proteins across eukaryotic membranes and in the cell contact- and calcium-dependent regulation of T3S [23].

Associations of yscD with chemical compounds

• The yersiniabactin (Ybt) system is a siderophore-dependent transport system required for full virulence [24].
• The active component of the proposed subunit vaccine combines the F1 capsular protein and V virulence antigen of Y. pestis and improves upon the design of an earlier histidine-tagged fusion protein [25].
• The differing virulence roles and functions have been attributed to minor sequence variations at the surface-exposed regions important for substrate recognition, to the dependence of omptin functions on lipopolysaccharide, and to the different regulation of omptin expression [26].

Other interactions of yscD

• In this study, we located and characterized the yopM gene to obtain clues about its role in the virulence of Y. pestis [1].
• The protein products of yscC, yscD, and yscG were identified and localized by immunoblot analysis [27].
• Together with an earlier study showing that a Y. pestis psaA mutant was reduced in virulence, these results demonstrate that the expression of fimbriae which are induced in host macrophages is involved in plague pathogenesis [28].
• The presence of a second flhA/lcrD homolog was not detected in Cj, indicating that a a separate homolog involved in secretion of virulence proteins may not be present [29].
• The altered lcrV was introduced into the low-Ca2+ response plasmid in Y. pestis by allelic exchange, and the resulting mutant was characterized for its two-dimensional protein profiles, growth, expression of an operon fusion to another low-Ca2+ response virulence operon, and virulence in mice [30].

Analytical, diagnostic and therapeutic context of yscD

• When mice were challenged by intraperitoneal injection both the mutant and the wild-type strain produced infections of similar virulence but mutant showed a slower rate of infection after oral challenge [31].
• A 9.5-kilobase plasmid of Yersinia pestis, the causative agent of plague, is required for high virulence when mice are inoculated with the bacterium by subcutaneous injection [9].
• By using Northern blot analyses we show that transcription of both fliA and flgM is immediately arrested when cells are exposed to 37 degrees C, coincident with the timing of virulence gene induction [32].
• Virulence in standard animal models (mice, rats, and guinea pigs) was not correlated with resistance to the bactericidal action of serum [33].
• The expression of polypeptides of the virulence plasmid of Yersinia enterocolitica serotype O:3 was studied with the immunoblotting technique and specifically absorbed antisera to Y. enterocolitica O:3 [34].

References