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Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells.

Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells. Research Abstract Details 

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  • Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells. Abstract Text:

    quynh t phanQuynh T Phan,carter l myersCarter L Myers,yue fuYue Fu,donald c sheppardDonald C Sheppard,michael r yeamanMichael R Yeaman,william h welchWilliam H Welch,ashraf s ibrahimAshraf S Ibrahim,john e edwardsJohn E Edwards,scott g fillerScott G Filler,

    Candida albicans is the most common cause of hematogenously disseminated and oropharyngeal candidiasis. Both of these diseases are characterized by fungal invasion of host cells. Previously, we have found that C. albicans hyphae invade endothelial cells and oral epithelial cells in vitro by inducing their own endocytosis. Therefore, we set out to identify the fungal surface protein and host cell receptors that mediate this process. We found that the C. albicans Als3 is required for the organism to be endocytosed by human umbilical vein endothelial cells and two different human oral epithelial lines. Affinity purification experiments with wild-type and an als3delta/als3delta mutant strain of C. albicans demonstrated that Als3 was required for C. albicans to bind to multiple host cell surface proteins, including N-cadherin on endothelial cells and E-cadherin on oral epithelial cells. Furthermore, latex beads coated with the recombinant N-terminal portion of Als3 were endocytosed by Chinese hamster ovary cells expressing human N-cadherin or E-cadherin, whereas control beads coated with bovine serum albumin were not. Molecular modeling of the interactions of the N-terminal region of Als3 with the ectodomains of N-cadherin and E-cadherin indicated that the binding parameters of Als3 to either cadherin are similar to those of cadherin-cadherin binding. Therefore, Als3 is a fungal invasin that mimics host cell cadherins and induces endocytosis by binding to N-cadherin on endothelial cells and E-cadherin on oral epithelial cells. These results uncover the first known fungal invasin and provide evidence that C. albicans Als3 is a molecular mimic of human cadherins.

    Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells. Publishing Authors By Initials

    qt phanQT Phan,cl myersCL Myers,y fuY Fu,dc sheppardDC Sheppard,mr yeamanMR Yeaman,wh welchWH Welch,as ibrahimAS Ibrahim,je edwardsJE Edwards,sg fillerSG Filler,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research

    PUBMED ID PMID:

    MEDLINE DATE:

    Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: PLoS biology

    VOLUME: 5

    Page Numbers: e64

    Journal Abbreviation: PLoS Biol.

    ISSN: 1545-7885

    DAY: 3

    MONTH: Mar

    YEAR: 2007

    Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 101183755

    Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells. Keywords Mesh Terms:

    KEYWORDS: Protein Binding

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells. Information

    Substance Name: Fungal Proteins

    Registry Number: 0

    Grant and Affiliation Information for Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells.

    AFFILIATION: Department of Medicine, Los Angeles Biomedical Research Institute, Harbor-UCLA Medical Center, Torrance, California, United States of America.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIDCR

    GRANT: R01DE017088

    ACRONYM: DE

    MEDLINETA: PLoS Biol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

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