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Infection and Immunity, November 2005, p. 7747-7758, Vol. 73, No. 11
0019-9567/05/$08.00+0 doi:10.1128/IAI.73.11.7747-7758.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Departments of Infectious Diseases, Infection Control, and Employee Health,1 Genitourinary Medical Oncology,2 Cancer Biology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas,3 College of Pharmacy, University of Houston, Houston, Texas4
Received 27 June 2005/ Accepted 27 July 2005
Invasive aspergillosis is a leading cause of infectious death in immunosuppressed patients. Here, we adapted a phage display library-based selection to screen and identify binding peptides to the surface of Aspergillus fumigatus conidia and hyphae. We identified a peptide (sequence CGGRLGPFC) that reliably binds to the surface of Aspergillus fumigatus hyphae. Binding was not Aspergillus strain specific, as it was also observed in hyphae of other Aspergillus clinical isolates. Furthermore, CGGRLGPFC-displaying phage targets Aspergillus fumigatus hyphae on formalin-fixed paraffin-embedded histopathology sections of lung tissue recovered from mice with invasive pulmonary aspergillosis. This approach may yield reagents such as peptidomimetics for novel diagnostic and therapeutic interventions in invasive aspergillosis.
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