Demonstration of fungal proteinase during phagocytosis of<i>Candida albicans</i>and<i>Candida tropicalis</i>

Borg, Margarete; Rüchel, R.

doi:10.1080/02681219080000021

Cited by 54 publications

(34 citation statements)

References 36 publications

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“…Moreover, they showed about a three-fold increase in germ tube formation within the cells in experiments without serum, as well as with inactivated and fresh serum. The germtube formation of C. albicans within the macrophages could indicate the inefficiency of the cells for blocking the yeast's growth (23)(24)(25). Spreading is an important mechanism of interaction between the phagocyte and the particle to be engulfed, and is employed largely to determine macrophage function and activation.…”

Section: Discussionmentioning

confidence: 99%

Long-Term Effect of Early Protein Malnutrition on Growth Curve, Hematological Parameters and Macrophage Function of Rats

Prestes-Carneiro

Laraya

Silva

et al. 2006

J Nutr Sci Vitaminol

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SummaryTo evaluate the long-term effect of mild-early maternal protein malnutrition on weight gain, hematological parameters and macrophage function in rats at adult age, we compared rats whose dams were fed diets containing either 9.5% (low protein-LPD) or 23% protein (normal-NPD) for the first 12 d of lactation. At 80 d of age, the functions of spreading, phagocytosis and killing Candida albicans were determined in resident peritoneal macrophages, whereas leukocytes and red blood cells were counted in peripheral blood. The number of resident peritoneal macrophages from LPD was the same as from NPD, but the ability of spreading and phagocytosing opsonised yeast was impaired. Besides, they were not able to block the germ tube formation or kill C. albicans to the same extent as in the control group. The low protein diet produced a significant reduction in the pups' growth and in hematological parameters although no difference was found in leukocyte counts. Taken together the data suggest that protein malnutrition during early lactation induces permanent alterations in macrophage function, body composition and hematological status, which are not restored completely even after a normal protein diet is supplied.

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Section: Discussionmentioning

confidence: 99%

Long-Term Effect of Early Protein Malnutrition on Growth Curve, Hematological Parameters and Macrophage Function of Rats

Prestes-Carneiro

Laraya

Silva

et al. 2006

J Nutr Sci Vitaminol

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“…37) These descriptions imply that the virulence of C. albicans is a function of multiple factors working jointly to overcome the host defenses. We suggest that the Candida extracellular proteinases are one of the important virulence factors, as already pointed out by several authors, [3][4][5][6][7][8][9][10]14,15,21,22,28,[34][35][36][37] though the relative importance differs with the strains because of the producibility in vivo. 14) Whether this similarity of AP for these serotypes (A and B) can be expanded to all other strains 38) remains to be investigated.…”

Section: )mentioning

confidence: 75%

“…11,12) It has been shown that the recovery of the serotype A strains was more pronounced than that of serotype B in mice when both strains were orally inoculated with mixtures of the two strains. 13) Borg and Rüchel 14) reported that different strains of serotype B, during infection into phagocytes, expressed an AP antigen only on blastoconidia, while filamentous cells of these strains appeared to be nonproteolytic, and that the serotype A strains expressed the antigen on the cells of both types.…”

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confidence: 99%

Similarity of Acid Proteinases Secreted by Candida albicans NIH A-207 and NIH B-792 Strains Cultured in BSA-Supplemented Medium

Okawa

Suzuki

Chiba

2005

Biological & Pharmaceutical Bulletin

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Candidosis is an endogenous infectious disease occurring in a compromised host. Among the various Candida species, C. albicans is the most medically important. In 1961, Hasenclever and Mitchell 1,2) identified two serotypes in C. albicans species, A and B, demonstrating that the pathogenicity of both types was identical in mice when the inoculation of the cells was conducted via the intravenous route. The acid proteinase (AP) produced by the C. albicans species has attracted a great deal of attention as a virulence factor in the pathogenesis of human and animal infections, [3][4][5][6][7][8][9][10] though the existence of contradictory findings has been pointed out. 11,12) It has been shown that the recovery of the serotype A strains was more pronounced than that of serotype B in mice when both strains were orally inoculated with mixtures of the two strains.13) Borg and Rüchel 14) reported that different strains of serotype B, during infection into phagocytes, expressed an AP antigen only on blastoconidia, while filamentous cells of these strains appeared to be nonproteolytic, and that the serotype A strains expressed the antigen on the cells of both types.During the course of screening the proteinase-producing Candida strains, we found that the C. albicans NIH B-792 (serotype B) strain produced a large amount of AP in the culture broth compared to the C. albicans NIH A-207 (serotype A) strain when cultured in a yeast carbon-based medium supplemented with bovine serum albumin (BSA) as the sole nitrogen source. In this paper, we have compared the properties of the APs produced by the C. albicans NIH A-207 and NIH B-792 strains in order to determine the relevance of these enzymes in Candidosis. MATERIALS AND METHODS Organisms and Growth Conditions C. albicans NIH A-207 (serotype A) and C. albicans NIH B-792 (serotype B)strains, abbreviated A-207 and B-792, respectively, were kindly donated by Dr. T. Shinoda, Department of Microbiology, Meiji College of Pharmacy, Tokyo, Japan, and were maintained on Sabouraud agar. The organisms were routinely inoculated into 200 ml of 0.5% (w/v) of Sabouraud medium supplemented with yeast extract, and cultured in a rotary shaker (150 rpm) for 48 h at 27 ЊC. After cultivation, the organisms were collected by centrifugation, and washed three times with saline. The washed cells (5ϫ10 8 ) were then suspended in 1 ml of saline. To obtain the secretory AP, 1 ml of the washed cell suspension was cultured in 200 ml of growth medium containing 0.2% BSA and a 1.17% yeast carbon base in a 500 ml culture flask, and then further cultured for 2-3 d at 27 ЊC on a rotary shaker (150 rpm).Assay of AP Activity AP activity was determined as described by Kobayashi et al. 15) using bovine hemoglobin as the substrate. Briefly, a 0.4 ml portion of enzyme solution was added to 2 ml of substrate solution [6 g of bovine hemoglobin (Wako Pure Chemical Industries, Ltd., Osaka, Japan) in 1 l of 50 mM sodium citrate buffer (pH 3.6)] and the mixture was incubated at 37 ЊC for 60 min. The reaction was stoppe...

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“…Although C. parapsilosis secretes a large amount of ACP in vitro, this species is much less invasive than C. albicans and C. tropicalis (Bistoni et al, 1984). This discrepancy could be related to the expression of ACP in macrophages after phagocytosis of yeast since C. albicans and C. tropicalis, but not C. parapsilosis, express ACP on the surface of yeast cells in macrophages after phagocytosis (Borg & Ruchel, 1990).…”

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confidence: 90%

Cloning and sequencing of two Candida parapsilosis genes encoding acid proteases

Viragh

Sanglard

Togni

et al. 1993

Journal of General Microbiology

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Candida parapsilosis secretes an inducible acid protease (ACP) when cultivated in the presence of bovine serum albumin as the sole nitrogen source. In order to clone the ACP gene (ACP) of C. parapsilosis, a genomic library was screened with C. tropicalis ACP as the probe. Two different ORFs, ACPR and ACPL, were found to hybridize with the C. tropicalis ACP. ACPR contained a DNA sequence in agreement with the N-terminal amino acid sequence of C. parapsilosis ACP isolated from culture supernatants. ACPR was shown to be expressed and functional in a C. tropicalis acid protease mutant (acp) and with SDS-PAGE the protein product showed the same mobility as the ACP secreted by C. parapsilosis. These results imply that ACPR encodes the C. parapsilosis ACP. The deduced amino acid sequence of ACPR is similar to the amino acid sequence of proteases of the pepsin family.As in the case of the C. tropicalis and C. albicans ACP, the 5' extremity of ACPR revealed a propeptide containing two Lys-Arg amino acid pairs that have been identified as peptidase processing sites in several yeast-secreted peptides and protein precursors. As judged from the deduced amino acid sequences, the ACPL product would be similar to that of ACPR; however, a protein corresponding to ACPL was not found in supernatants from C. parapsilosis liquid cultures. In addition, ACPL did not complement the C. tropicalis acp mutant. We conclude that ACPL is a pseudogene or serves an as yet unidentified function.

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Demonstration of fungal proteinase during phagocytosis ofCandida albicansandCandida tropicalis

Cited by 54 publications

References 36 publications

Long-Term Effect of Early Protein Malnutrition on Growth Curve, Hematological Parameters and Macrophage Function of Rats

Long-Term Effect of Early Protein Malnutrition on Growth Curve, Hematological Parameters and Macrophage Function of Rats

Similarity of Acid Proteinases Secreted by Candida albicans NIH A-207 and NIH B-792 Strains Cultured in BSA-Supplemented Medium

Cloning and sequencing of two Candida parapsilosis genes encoding acid proteases

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