Protein targets for broad-spectrum mycosis vaccines: quantitative proteomic analysis of Aspergillus and Coccidioides and comparisons with other fungal pathogens

• Published in: Annals of the New York Academy of Sciences Vol. 1273; no. 1; pp. 44 - 51
• Main Authors: Champer, Jackson, Diaz-Arevalo, Diana, Champer, Miriam, Hong, Teresa B., Wong, Mayyen, Shannahoff, Molly, Ito, James I., Clemons, Karl V., Stevens, David A., Kalkum, Markus
• Format: Journal Article
• Language: English
• Published: Malden, USA Blackwell Publishing Inc 01.12.2012; Wiley Subscription Services, Inc
• Subjects: Aspergillus; Aspergillus - immunology; Aspergillus - metabolism; Aspergillus fumigatus; Coccidioides; Coccidioides - immunology; Coccidioides - metabolism; Composting; Fungal Proteins - immunology; Fungal Vaccines - immunology; Fungi; Homology; Indoor air quality; Mass Spectrometry; panfungal vaccine; Pathogens; Proteins; Proteome; quantitative proteomics; Receiving; Vaccines; Valleys
• ISSN: 0077-8923; 1749-6632
• DOI: 10.1111/j.1749-6632.2012.06761.x

Aspergillus species are responsible for most cases of fatal mold infections in immunocompromised patients, particularly in those receiving hematopoietic stem cell transplants. Experimental vaccines in mouse models have demonstrated a promising avenue of approach for the prevention of aspergillosis, as well as infections caused by other fungal pathogens, such as Coccidioides, the etiological agent of valley fever (coccidioidomycosis). Here, we investigated the hyphal proteomes of Aspergillus fumigatus and Coccidioides posadasii via quantitative MSE mass spectrometry with the objective of developing a vaccine that cross‐protects against these and other species of fungi. Several homologous proteins with highly conserved sequences were identified and quantified in A. fumigatus and C. posadasii. Many abundant proteins from the cell wall of A. fumigatus present themselves as possible cross‐protective vaccine candidates, due to the high degree of sequence homology to other medically relevant fungal proteins and low homologies to human or murine proteins.