Vitronectin interacts with Candida albicans and augments organism attachment to the NR8383 macrophage cell line

Andrew H. Limper; Joseph E. Standing

doi:10.1016/0165-2478(94)90077-9

Vitronectin interacts with Candida albicans and augments organism attachment to the NR8383 macrophage cell line

Andrew H. Limper, Joseph E. Standing

Pulmonary and Critical Care Medicine

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

Candida albicans is an increasingly important cause of mucocutaneous and bloodstream infections. The potential role of circulating adhesive glycoproteins such as vitronectin (Vn) in host defense against C. albicans is currently unknown. Accordingly, we investigated the binding of plasma-derived Vn with C. albicans strain 36082. Vn specifically bound to C. albicans in a concentration-dependent fashion. Higher affinity binding sites numbered 9.8 × 10⁴ sites per organism, with a dissociation constant, K_d of 3.5 × 10^-7M. Vn binding with C. albicans was significantly inhibited by heparin, suggesting interaction of the organism with Vn's glycosaminoglycan-binding region. To further determine which molecule(s) on the fungus interacted with Vn, C. albicans components were extracted, separated by SDS and blotted with radiolabeled Vn. These studies revealed that Vn binds to a 30 kDa molecule on C. albicans. Finally, we investigated the role of Vn in promoting interaction of C. albicans with phagocytic cells. Incubation of C. albicans in the presence of Vn significantly increased binding of the organism to cultured NR8383 macrophages compared to incubations performed in the absence of Vn. These data demonstrate that C. albicans interacts with the heparin-binding domain Vn and further suggest that Vn augments organism uptake by phagocytic cells.

Original language	English (US)
Pages (from-to)	139-144
Number of pages	6
Journal	Immunology Letters
Volume	42
Issue number	3
DOIs	https://doi.org/10.1016/0165-2478(94)90077-9
State	Published - Oct 1994

Keywords

Adherence
Candida albicans
Heparin
Macrophage
Vitronectin

ASJC Scopus subject areas

Immunology and Allergy
Immunology

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10.1016/0165-2478(94)90077-9

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title = "Vitronectin interacts with Candida albicans and augments organism attachment to the NR8383 macrophage cell line",

abstract = "Candida albicans is an increasingly important cause of mucocutaneous and bloodstream infections. The potential role of circulating adhesive glycoproteins such as vitronectin (Vn) in host defense against C. albicans is currently unknown. Accordingly, we investigated the binding of plasma-derived Vn with C. albicans strain 36082. Vn specifically bound to C. albicans in a concentration-dependent fashion. Higher affinity binding sites numbered 9.8 × 104 sites per organism, with a dissociation constant, Kd of 3.5 × 10-7M. Vn binding with C. albicans was significantly inhibited by heparin, suggesting interaction of the organism with Vn's glycosaminoglycan-binding region. To further determine which molecule(s) on the fungus interacted with Vn, C. albicans components were extracted, separated by SDS and blotted with radiolabeled Vn. These studies revealed that Vn binds to a 30 kDa molecule on C. albicans. Finally, we investigated the role of Vn in promoting interaction of C. albicans with phagocytic cells. Incubation of C. albicans in the presence of Vn significantly increased binding of the organism to cultured NR8383 macrophages compared to incubations performed in the absence of Vn. These data demonstrate that C. albicans interacts with the heparin-binding domain Vn and further suggest that Vn augments organism uptake by phagocytic cells.",

keywords = "Adherence, Candida albicans, Heparin, Macrophage, Vitronectin",

author = "Limper, {Andrew H.} and Standing, {Joseph E.}",

note = "Funding Information: This work was gerenously supported by funds from the National Institutes of Health (NIH R29 AI34336-01) and from American Lung Association (Research Grant RG-011-N). This work was performed during the tenure of a Clinician-Scientist Award from the American Heart Association (to A.H.L.). The authors thank Ronald Helmke for his gift of NR8383 cells and Kathy Streich for assistance in preparing the final manuscript.",

year = "1994",

month = oct,

doi = "10.1016/0165-2478(94)90077-9",

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T1 - Vitronectin interacts with Candida albicans and augments organism attachment to the NR8383 macrophage cell line

AU - Limper, Andrew H.

AU - Standing, Joseph E.

N1 - Funding Information: This work was gerenously supported by funds from the National Institutes of Health (NIH R29 AI34336-01) and from American Lung Association (Research Grant RG-011-N). This work was performed during the tenure of a Clinician-Scientist Award from the American Heart Association (to A.H.L.). The authors thank Ronald Helmke for his gift of NR8383 cells and Kathy Streich for assistance in preparing the final manuscript.

PY - 1994/10

Y1 - 1994/10

N2 - Candida albicans is an increasingly important cause of mucocutaneous and bloodstream infections. The potential role of circulating adhesive glycoproteins such as vitronectin (Vn) in host defense against C. albicans is currently unknown. Accordingly, we investigated the binding of plasma-derived Vn with C. albicans strain 36082. Vn specifically bound to C. albicans in a concentration-dependent fashion. Higher affinity binding sites numbered 9.8 × 104 sites per organism, with a dissociation constant, Kd of 3.5 × 10-7M. Vn binding with C. albicans was significantly inhibited by heparin, suggesting interaction of the organism with Vn's glycosaminoglycan-binding region. To further determine which molecule(s) on the fungus interacted with Vn, C. albicans components were extracted, separated by SDS and blotted with radiolabeled Vn. These studies revealed that Vn binds to a 30 kDa molecule on C. albicans. Finally, we investigated the role of Vn in promoting interaction of C. albicans with phagocytic cells. Incubation of C. albicans in the presence of Vn significantly increased binding of the organism to cultured NR8383 macrophages compared to incubations performed in the absence of Vn. These data demonstrate that C. albicans interacts with the heparin-binding domain Vn and further suggest that Vn augments organism uptake by phagocytic cells.

AB - Candida albicans is an increasingly important cause of mucocutaneous and bloodstream infections. The potential role of circulating adhesive glycoproteins such as vitronectin (Vn) in host defense against C. albicans is currently unknown. Accordingly, we investigated the binding of plasma-derived Vn with C. albicans strain 36082. Vn specifically bound to C. albicans in a concentration-dependent fashion. Higher affinity binding sites numbered 9.8 × 104 sites per organism, with a dissociation constant, Kd of 3.5 × 10-7M. Vn binding with C. albicans was significantly inhibited by heparin, suggesting interaction of the organism with Vn's glycosaminoglycan-binding region. To further determine which molecule(s) on the fungus interacted with Vn, C. albicans components were extracted, separated by SDS and blotted with radiolabeled Vn. These studies revealed that Vn binds to a 30 kDa molecule on C. albicans. Finally, we investigated the role of Vn in promoting interaction of C. albicans with phagocytic cells. Incubation of C. albicans in the presence of Vn significantly increased binding of the organism to cultured NR8383 macrophages compared to incubations performed in the absence of Vn. These data demonstrate that C. albicans interacts with the heparin-binding domain Vn and further suggest that Vn augments organism uptake by phagocytic cells.

KW - Adherence

KW - Candida albicans

KW - Heparin

KW - Macrophage

KW - Vitronectin

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JO - Immunology Letters

JF - Immunology Letters

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ER -

Vitronectin interacts with Candida albicans and augments organism attachment to the NR8383 macrophage cell line

Abstract

Keywords

ASJC Scopus subject areas

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