{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T22:37:26Z","timestamp":1790203046016,"version":"4.1.0"},"reference-count":78,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T00:00:00Z","timestamp":1783468800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T00:00:00Z","timestamp":1783468800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI148561, R21AI190214"],"award-info":[{"award-number":["R01AI148561, R21AI190214"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2026,7,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      During infection,\n                      <jats:italic toggle=\"yes\">Histoplasma capsulatum<\/jats:italic>\n                      exists primarily as an intracellular pathogen of phagocytes, where it overcomes host defense mechanisms and replicates within the phagosome. This intracellular proliferation of\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      yeasts requires the function of the fungal peroxisome for multiple, incompletely defined roles, with early pathogenesis functions dependent on the proper trafficking of peroxisomal matrix proteins carrying a type 1 peroxisome-targeting signal (PTS1). To better understand the potential roles of peroxisomes during\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      infection, we identified the constituents of the peroxisomal proteome of pathogenic-phase\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      yeasts through proximity labeling using a peroxisome-targeted TurboID biotin ligase. Comparative proteomics using peroxisome- or cytosol-localized TurboID identified 90 high-confidence peroxisomal proteins. To validate the peroxisomal proteome, a subset of nine putative peroxisomal proteins was localized to the peroxisome using fluorescent protein fusions. Comparison of peroxisomal proteomes for\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      yeasts lacking the Pex5 or Pex7 cytosolic PTS1 or PTS2 receptors assigned proteins to either the PTS1- or PTS2-dependent peroxisomal import pathways, and refined the Histoplasma PTS1 tripeptide consensus sequence. The peroxisomal proteome of\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      yeast during macrophage infection was ultimately determined to provide relevance to\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      \u2019s primary pathogenic niche. The identities of the proteins comprising the peroxisomal proteome include several enzymes for canonical peroxisome-localized biochemical pathways (e.g., fatty acid utilization and siderophore biosynthesis), but also represent several potential novel functions for the organelle. The defined peroxisomal proteome of pathogenic-phase\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      yeasts, particularly the set of proteins imported via the PTS1 import pathway, thus establishes the important foundation for understanding how peroxisomes promote intracellular pathogenesis.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>\n                      Peroxisomes are eukaryotic organelles that serve as a subcellular compartment for diverse metabolic and biosynthetic reactions, some of which play crucial roles in supporting the intracellular pathogenesis of the fungal pathogen\n                      <jats:italic toggle=\"yes\">Histoplasma capsulatum<\/jats:italic>\n                      . In this study, we used proximity labeling with the biotin ligase TurboID to capture peroxisomal matrix proteins, enabling the empirical derivation of the peroxisomal proteome of pathogenic-phase\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      yeasts, including during\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      infection of mammalian cells. This represents the first organelle-specific proteome definition in\n                      <jats:italic toggle=\"yes\">Histoplasma<\/jats:italic>\n                      and highlights the utility of proximity-based biotinylation and comparative proteomics for understanding how subcellular compartments and their functions contribute to intracellular pathogenesis.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.00771-26","type":"journal-article","created":{"date-parts":[[2026,6,9]],"date-time":"2026-06-09T13:00:28Z","timestamp":1781010028000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":1,"title":["Determination of the peroxisomal proteome of pathogenic stage\n                    <i>Histoplasma capsulatum<\/i>"],"prefix":"10.1128","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-7632-3725","authenticated-orcid":false,"given":"Peter 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