인문학
사회과학
자연과학
공학
의약학
농수해양학
예술체육학
복합학
DBpia AI
AI 에이전트
AI 아이디어
AI 리더
AI 뷰어
Citeasy
크롬 서지관리 다운로드
지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
Candida glabrata (currently classified as Nakaseomyces glabratus) is an opportunistic yeast-like fungus that causes infections in humans, with limited treatment options due to resistance to antifungal drugs. In contrast to C. albicans, which produces secreted aspartic proteases (Saps) involved in pathogenicity, C. glabrata expresses a distinct group of cell surface-associated aspartic proteases known as yapsins (Yps). While YPS gene deletion mutants have proposed roles in cellular homeostasis, their precise contribution to fungal virulence and host interactions remains unclear. Herein, we present the first detailed biochemical and functional characterization of two native Yps proteins, Yps3 and Yps9, purified from C. glabrata cultures. Both proteases displayed robust activity in a mildly acidic to neutral pH range (5.5-7.0), resistance to the classical aspartic protease inhibitor pepstatin A, and selectively degraded key host antimicrobial peptides, including LL-37 cathelicidin, histatin 5 (Hst5), and kininogen-derived peptide NAT26, by hydrolyzing lysine residues. Additionally, Yps9 promoted C. albicans biofilm dispersal. In a Galleria mellonella infection model, a pre-treatment with each protease enhanced larval survival and increased phenol oxidase activity, implying a role of yapsins in immune priming. Collectively, these findings reveal multifunctional roles for Yps3 and Yps9 in fungal virulence, biofilm modulation, and host immune interactions.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
최근 본 자료 전체보기
