Matos Baltazar Ludmila, Nakayasu Ernesto S, Sobreira Tiago J P, Choi Hyungwon, Casadevall Arturo, Nimrichter Leonardo, Nosanchuk Joshua D
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA; Division of Infectious Diseases, Department of Medicine, Albert Einstein College of Medicine, Bronx, New York, USA.
Biological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington, USA; Bindley Bioscience Center, Purdue University, West Lafayette, Indiana, USA.
mSphere. 2016 Mar 30;1(2). doi: 10.1128/mSphere.00085-15. eCollection 2016 Mar-Apr.
Histoplasma capsulatum produces extracellular vesicles containing virulence-associated molecules capable of modulating host machinery, benefiting the pathogen. Treatment of H. capsulatum cells with monoclonal antibodies (MAbs) can change the outcome of infection in mice. We evaluated the sizes, enzymatic contents, and proteomic profiles of the vesicles released by fungal cells treated with either protective MAb 6B7 (IgG1) or nonprotective MAb 7B6 (IgG2b), both of which bind H. capsulatum heat shock protein 60 (Hsp60). Our results showed that treatment with either MAb was associated with changes in size and vesicle loading. MAb treatments reduced vesicle phosphatase and catalase activities compared to those of vesicles from untreated controls. We identified 1,125 proteins in vesicles, and 250 of these manifested differences in abundance relative to that of proteins in vesicles isolated from yeast cells exposed to Hsp60-binding MAbs, indicating that surface binding of fungal cells by MAbs modified protein loading in the vesicles. The abundance of upregulated proteins in vesicles upon MAb 7B6 treatment was 44.8% of the protein quantities in vesicles from fungal cells treated with MAb 6B7. Analysis of orthologous proteins previously identified in vesicles from other fungi showed that different ascomycete fungi have similar proteins in their extracellular milieu, many of which are associated with virulence. Our results demonstrate that antibody binding can modulate fungal cell responses, resulting in differential loading of vesicles, which could alter fungal cell susceptibility to host defenses. This finding provides additional evidence that antibody binding modulates microbial physiology and suggests a new function for specific immunoglobulins through alterations of fungal secretion. IMPORTANCE Diverse fungal species release extracellular vesicles, indicating that this is a common pathway for the delivery of molecules to the extracellular space. However, there has been no study reporting the impact of antibody binding to the fungal cell on extracellular vesicle release. In the present work, we observed that treatment of H. capsulatum cells with Hsp60-binding MAbs significantly changed the size and cargo of extracellular vesicles, as well as the enzymatic activity of certain virulence factors, such as laccase and phosphatase. Furthermore, this finding demonstrates that antibody binding can directly impact protein loading in vesicles and fungal metabolism. Hence, this work presents a new role for antibodies in the modification of fungal physiology.
荚膜组织胞浆菌产生含有能够调节宿主机制的毒力相关分子的细胞外囊泡,这对病原体有益。用单克隆抗体(MAb)处理荚膜组织胞浆菌细胞可改变小鼠的感染结果。我们评估了用保护性单克隆抗体6B7(IgG1)或非保护性单克隆抗体7B6(IgG2b)处理的真菌细胞释放的囊泡的大小、酶含量和蛋白质组学特征,这两种抗体均与荚膜组织胞浆菌热休克蛋白60(Hsp60)结合。我们的结果表明,用任何一种单克隆抗体处理都与囊泡大小和囊泡负载的变化有关。与未处理对照的囊泡相比,单克隆抗体处理降低了囊泡磷酸酶和过氧化氢酶活性。我们在囊泡中鉴定出1125种蛋白质,其中250种蛋白质相对于从暴露于Hsp60结合单克隆抗体的酵母细胞中分离的囊泡中的蛋白质丰度表现出差异,这表明单克隆抗体与真菌细胞的表面结合改变了囊泡中的蛋白质负载。单克隆抗体7B6处理后囊泡中上调蛋白质的丰度是用单克隆抗体6B7处理的真菌细胞囊泡中蛋白质数量的44.8%。对先前在其他真菌的囊泡中鉴定出的直系同源蛋白质的分析表明,不同的子囊菌在其细胞外环境中具有相似的蛋白质,其中许多与毒力相关。我们的结果表明,抗体结合可调节真菌细胞反应,导致囊泡负载差异,这可能改变真菌细胞对宿主防御的敏感性。这一发现提供了额外的证据,证明抗体结合可调节微生物生理学,并通过改变真菌分泌提示特定免疫球蛋白的新功能。重要性多种真菌物种释放细胞外囊泡,这表明这是将分子递送到细胞外空间的常见途径。然而,尚无研究报道抗体与真菌细胞结合对细胞外囊泡释放的影响。在本研究中,我们观察到用Hsp60结合单克隆抗体处理荚膜组织胞浆菌细胞显著改变了细胞外囊泡的大小和货物,以及某些毒力因子如漆酶和磷酸酶的酶活性。此外,这一发现表明抗体结合可直接影响囊泡中的蛋白质负载和真菌代谢。因此,这项工作揭示了抗体在真菌生理学修饰中的新作用。