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Passive Administration of Monoclonal Antibodies Against H. capsulatum and Others Fungal Pathogens
Published on: February 14, 2011
Antibody Binding Alters the Characteristics and Contents of Extracellular Vesicles Released by Histoplasma capsulatum
Ludmila Matos Baltazar1, Ernesto S Nakayasu2, Tiago J P Sobreira3
1Department 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.
Abstract:
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.
Insights
Monoclonal antibodies (MAbs) targeting Histoplasma capsulatum heat shock protein 60 altered the size and protein cargo of extracellular vesicles. This antibody binding modulates fungal physiology and vesicle secretion, impacting host-pathogen interactions.
Area of Science:
- Mycology
- Immunology
- Cell Biology
Background:
- Histoplasma capsulatum releases extracellular vesicles containing virulence factors.
- Monoclonal antibodies (MAbs) can influence fungal infection outcomes.
- Heat shock protein 60 (Hsp60) is a target for MAbs against H. capsulatum.
Purpose of the Study:
- To investigate how protective (MAb 6B7) and nonprotective (MAb 7B6) MAbs targeting H. capsulatum Hsp60 affect the properties of fungal extracellular vesicles.
- To analyze changes in vesicle size, enzymatic content, and proteomic profiles upon MAb treatment.
Main Methods:
- Treatment of H. capsulatum cells with specific MAbs (6B7 and 7B6).
- Isolation and characterization of extracellular vesicles.
- Analysis of vesicle size, enzymatic activities (phosphatase, catalase), and proteomic profiles.
- Quantitative proteomics to identify differentially abundant proteins.
Main Results:
- MAb treatment altered vesicle size and protein loading compared to untreated controls.
- Vesicles from MAb-treated cells showed reduced phosphatase and catalase activity.
- Proteomic analysis identified significant differences in protein cargo, with 250 proteins showing altered abundance.
- MAb 7B6 treatment resulted in a higher abundance of upregulated proteins in vesicles compared to MAb 6B7 treatment.
Conclusions:
- Antibody binding to H. capsulatum cells modulates fungal extracellular vesicle composition and enzymatic activity.
- Differential protein loading in vesicles can impact fungal susceptibility to host defenses.
- This study reveals a novel role for antibodies in altering fungal physiology and secretion pathways.
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