Project Title

Microsporidial Attachment and Host Cell Signaling

Authors' Affiliations

Cindy Barrett, Department of Biomedical Science, Quillen College of Medicine, East Tennessee State University, Johnson City, TN Dr. Russell Hayman, Department of Biomedical Science, Quillen College of Medicine, East Tennessee State University, Johnson City, TN Cheryl Moore, Department of Biomedical Science, Quillen College of Medicine, East Tennessee State University, Johnson City, TN

Faculty Sponsor’s Department

Biomedical Sciences

Type

Oral Non-Competitive

Classification of First Author

Graduate Student-Doctoral

Project's Category

Biological Sciences, Cell Biology, AIDS

Abstract Text

Microsporidia exploit several targets for binding to host cells. Attachment is known to be an important first step before infection, and by blocking attachment, host cell infection decreases. This project seeks to determine if microsporidia use an ADAM (A Disintegrin And Metalloprotease) like protein to bind to host integrins. To test this, spore adherence assays employed a small, generated peptide that selected the integrin binding domain of the ADAM like protein. Afterwards, spore attachment to cell culture was quantified to determine if the peptide blocked spore attachment to cell monolayers. This project expands previous work by testing attachment of an additional microsporidia species. Finally, cell lysates pretreated with the peptide were screened for phosphorylation of FAK (Focal Adhesion Kinase), a common signaling pathway for activated integrins. Preliminary results suggest that microsporidial ADAM peptides bind to host cell integrins to decrease spore adherence and induce host cell signaling under the FAK pathway.

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Microsporidial Attachment and Host Cell Signaling

Microsporidia exploit several targets for binding to host cells. Attachment is known to be an important first step before infection, and by blocking attachment, host cell infection decreases. This project seeks to determine if microsporidia use an ADAM (A Disintegrin And Metalloprotease) like protein to bind to host integrins. To test this, spore adherence assays employed a small, generated peptide that selected the integrin binding domain of the ADAM like protein. Afterwards, spore attachment to cell culture was quantified to determine if the peptide blocked spore attachment to cell monolayers. This project expands previous work by testing attachment of an additional microsporidia species. Finally, cell lysates pretreated with the peptide were screened for phosphorylation of FAK (Focal Adhesion Kinase), a common signaling pathway for activated integrins. Preliminary results suggest that microsporidial ADAM peptides bind to host cell integrins to decrease spore adherence and induce host cell signaling under the FAK pathway.

Project Video