Sialic Acid-Dependent Recognition of Laminin by
            <i>Penicillium marneffei</i>
            Conidia

Hamilton, Andrew J.; Jeavons, L.; Youngchim, Sirida; Vanittanakom, Nongnuch; Hay, R. J.

doi:10.1128/iai.66.12.6024-6026.1998

Cited by 57 publications

(31 citation statements)

References 16 publications

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“…Organism and culture conditions. P. marneffei ATCC 200051 was grown in the mycelial phase on Sabouraud dextrose agar slopes at 30°C, and conidia were obtained from 8-day-old cultures as previously described (10). Conidia were quantified in a hemocytometer.…”

Section: Methodsmentioning

confidence: 99%

“…The latter are thought to be sufficiently small to reach the alveoli. Virtually nothing is known of the pathogenic mechanisms responsible for the development of infection following conidial inhalation, although recently P. marneffei conidia have been shown to bind laminin via a sialic acid-dependent process (10). Laminin is an important extracellular matrix (ECM) glycoprotein (12) that is present in basement membranes, and it may become exposed after tissue damage.…”

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confidence: 99%

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Recognition of Fibronectin by Penicillium marneffei Conidia via a Sialic Acid-Dependent Process and Its Relationship to the Interaction Between Conidia and Laminin

et al. 1999

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Adhesion of Penicillium marneffei conidia to the extracellular matrix protein laminin via a sialic acid-dependent process has previously been demonstrated. This study describes the interaction of P. marneffei conidia with fibronectin and examines the relationship of this process to the recognition of laminin via conidia. Immunofluorescence microscopy demonstrated that fibronectin bound to the surface of conidia and to phialides, but not to hyphae, in a pattern similar to that reported for laminin. Conidia were able to bind to fibronectin immobilized on microtiter plates in a concentration-dependent manner. However, binding to fibronectin (at any given concentration of protein and conidia) was less than that to laminin under equivalent conditions. Soluble fibronectin and antifibronectin antibody inhibited adherence of conidia to fibronectin in the plate adherence assay; soluble laminin also caused pronounced inhibition. Various monosaccharides and several peptides had no effect on adherence to fibronectin. However, N-acetylneuraminic acid abolished adherence to fibronectin, indicating that the interaction was mediated through a sialic acid-dependent process; the latter parallels observations of laminin binding by conidia. Fibronectin binding (and binding of laminin) was considerably reduced by prolonged preincubation of conidia with chymotrypsin, suggesting the protein nature of the binding site. Conidia from older cultures were more adherent to both immobilized fibronectin and laminin than conidia from younger cultures. Ligand affinity binding demonstrated the presence of a 20-kDa protein with the ability to bind both fibronectin and laminin. There would therefore appear to be a common receptor for the binding of fibronectin and laminin on the surface of P. marneffei, and the interaction described here maybe important in mediating attachment of the fungus to host tissue.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

Recognition of Fibronectin by Penicillium marneffei Conidia via a Sialic Acid-Dependent Process and Its Relationship to the Interaction Between Conidia and Laminin

et al. 1999

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“…are initially white and become blue-green, gray-green, olive-gray, yellow or pinkish with time [10]. Sialic acid specific lectin activity has been reported from P. marneffei which mediates its adhesion to host cells [11]. Literature survey reveals no report on lectin activity in penicilli.…”

Section: Introduction *mentioning

confidence: 99%

“…As yet penicilli, with an exception of P. marneffei [11], were not investigated for lectin activity. This is the first report on lectin activity from P. griseofulvum and P. thomii.…”

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Screening of Penicillium species for occurrence of lectins and their characterization

Singh

Sharma

Kaur

et al. 2009

J. Basic Microbiol.

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Out of 15 Penicillium species screened for lectin activities, P. griseofulvum and P. thomii were found to possess mycelial lectin activity. None of the species displayed extracellular or cell surface-bound lectin activity. Both species agglutinated rabbit erythrocytes. P. griseofulvum lectin showed specificity to human type O erythrocytes. While P. thomii lectin specifically agglutinated human type A erythrocytes. Highest lectin activities from P. thomii and P. griseofulvum were expressed after 8 and 7 days of growth, respectively. Lectins from both the species displayed a high binding affinity to chondroitin-6-sulphate, mucin, asialofetuin, D-sucrose, and D-trehalose. Ammonium sulphate at 50% saturation yielded 80% of the total lectin activity. Dialysis and ultrafiltration of the precipitates resulted in 1.79 and 3.46 fold purification of P. griseofulvum and P. thomii lectins, respectively. Both lectins showed pH optima between 7.0-8.0 and were stable near the neutral pH after 2 h. P. thomii lectin exhibited optimal activity at 35-40 degrees C, and P. griseofulvum lectin at 30-40 degrees C. P. thomii lectin showed a complete loss of activity above 40 degrees C, P. griseofulvum lectin was stable at or below 35 degrees C.

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“…The interaction of ECMp with various infectious agents has been reported, where these ECMp could serve as adherence substrates (Silva-Filho et al, 1988;Furtado et al, 1992;Li et al, 1995;Gaur et al, 1999;Wasylnka & Moore, 2000). Of particular interest in this context is the identification of ECM-binding proteins on the surface of several fungi of clinical importance such as Candida albicans (López-Ribot et al, 1996;Gaur et al, 1999), Aspergillus fumigatus (Coulot et al, 1994;Gil et al, 1996;Wasylnka & Moore, 2000), Histoplasma capsulatum (McMahon et al, 1995), Cryptococcus neoformans (Rodrigues et al, 2003), Pneumocystis carinii (Narasimhan et al, 1994), Sporothrix schenckii (Lima et al, 2001) and Penicillium marneffei (Hamilton et al, 1998(Hamilton et al, , 1999.…”

Section: Introductionmentioning

confidence: 99%

Involvement of extracellular matrix proteins in the course of experimental paracoccidioidomycosis

González

Gómez

Muñoz

et al. 2008

FEMS Immunology &Amp; Medical Microbiology

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We aimed at determining involvement of extracellular matrix proteins (ECMp) and an ECM-binding adhesin (32-kDa protein) from Paracoccidioides brasiliensis, in the course of experimental paracoccidioidomycosis. BALB/c mice were infected with P. brasiliensis conidia previously incubated with soluble laminin, fibronectin and fibrinogen or a mAb against the fungal adhesin. Inflammatory response, chitin levels and cytokine production at different postinfection periods were determined. Chitin was significantly decreased in lungs of mice infected with ECMp-treated conidia when compared with controls at week 8, especially with laminin and fibrinogen. Contrariwise, when animals were infected with mAb-treated conidia no differences in chitin content were found. The observed inflammatory reaction in lungs was equivalent in all cases. IFN-gamma increased significantly in lungs from mice infected with soluble ECMp - (at day 4 and week 12) or mAb-treated conidia (at week 12) when compared with animals infected with untreated conidia. Significant increased levels of tumour necrosis factor-alpha were observed at 8 weeks in animals infected with ECMp-treated conidia while no differences were observed during the remaining periods. These findings point toward an inhibitory effect of ECMp on P. brasiliensis conidia infectivity and suggest that these proteins may interfere with conidia initial adhesion to host tissues probably modulating the immune response in paracoccidioidomycosis.

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Sialic Acid-Dependent Recognition of Laminin by Penicillium marneffei Conidia

Cited by 57 publications

References 16 publications

Recognition of Fibronectin by Penicillium marneffei Conidia via a Sialic Acid-Dependent Process and Its Relationship to the Interaction Between Conidia and Laminin

Recognition of Fibronectin by Penicillium marneffei Conidia via a Sialic Acid-Dependent Process and Its Relationship to the Interaction Between Conidia and Laminin

Screening of Penicillium species for occurrence of lectins and their characterization

Involvement of extracellular matrix proteins in the course of experimental paracoccidioidomycosis

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