Biochimie 1996, 78:364–369 PubMedCrossRef 49 Kamaguchi A, Nakano

Biochimie 1996, 78:364–369.PubMedCrossRef 49. Kamaguchi A, Nakano M, Shoji M, Nakamura R, Sagane Y, Okamoto M, Watanabe T, Ohyama T, Ohta M, Nakayama K: Autolysis of Porphyromonas gingivalis is accompanied by an increase in several periodontal pathogenic factors in the supernatant. Microbiol Immunol 2004, 48:541–545.PubMed 50. Capestany CA, Kuboniwa M, Jung IY, Park Y, Tribble GD, Lamont RJ: Role of the Porphyromonas gingivalis InlJ protein

in homotypic and heterotypic biofilm development. Infect Immun 2006, 74:3002–3005.PubMedCrossRef Authors’ contributions TO conceived the study, contributed to its design, laboratory experiments, and data analysis selleck chemicals and wrote the manuscript. HW, JC, and MO contributed to the design, laboratory experiments, and the writing of the manuscript. All authors have read and approved the final manuscript.”
“Background C. albicans SUR7 shares 44% identity and 65% similarity with S. cerevisiae SUR7. S. cerevisiae SUR7 encodes a predicted integral membrane protein with an N-terminal AZD1152 price signal sequence and four transmembrane domains, and is a member of a family of proteins that also includes Yn1194p, Ydl222p, and Ylr414cp [1, 2]. Sur7p localizes to large, immobile, stable cortical patches on the plasma membrane, termed “”eisosomes”" which mark sites

of endocytosis [3, 4]. Deletion of S. cerevisiae SUR7 resulted in a strain with a defect in sporulation and altered plasma membrane sphingolipid content [4]. Alvarez and Konopka [5] identified C. albicans Sur7p in a detergent-resistant fraction of the plasma membrane in a proteomics study on N-acetylglucosamine-induced buy Everolimus proteins. Recently, they generated a C. albicans sur7Δ knockout mutant which is characterized by aberrant cell wall organization [2]. Specifically, lack of SUR7 in C. albicans results in mislocalization of actin and septin, and abnormal cell wall material protruding into and forming structures within the cytoplasm. However, from a phenotypic standpoint, little is known

regarding the role of C. albicans SUR7 in pathogenesis. A number of C. albicans virulence-related secreted proteins that remain associated with the plasma membrane or cell wall have been identified, including the outer mannoprotein Hwp1p [6], adhesins encoded by the ALS family of genes [7], and membrane proteins encoded by the Palbociclib pH-responsive genes PHR1 and PHR2 [8–11]. However, a genome-wide understanding of Candida secretory pathway proteins and virulence is still limited. Previously, we took advantage of SignalP v2.0 [12, 13] and a series of additional validated predictive algorithms to define a computational secretome of C. albicans from its entire genome [14]. In addition to identifying putative soluble secretory proteins, we also identified a number of putative and known membrane and cell-wall associated proteins [14]. We next compared these databases with published genome-wide expression profiling data to identify candidate virulence-related genes.

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