Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes
Abstract Background The Leishmania spp. protozoa are introduced into humans through a sand fly blood meal, depositing the infectious metacyclic promastigote form of the parasite into human skin. Parasites enter a variety of host cells, although a majority are found in macrophages where they replicat...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2018-06-01
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| Series: | Parasites & Vectors |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1186/s13071-018-2937-y |
| _version_ | 1818264540446457856 |
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| author | Skye Marshall Patrick H. Kelly Brajesh K. Singh R. Marshall Pope Peter Kim Bayan Zhanbolat Mary E. Wilson Chaoqun Yao |
| author_facet | Skye Marshall Patrick H. Kelly Brajesh K. Singh R. Marshall Pope Peter Kim Bayan Zhanbolat Mary E. Wilson Chaoqun Yao |
| author_sort | Skye Marshall |
| collection | DOAJ |
| description | Abstract Background The Leishmania spp. protozoa are introduced into humans through a sand fly blood meal, depositing the infectious metacyclic promastigote form of the parasite into human skin. Parasites enter a variety of host cells, although a majority are found in macrophages where they replicate intracellularly during chronic leishmaniasis. Symptomatic leishmaniasis causes considerable human morbidity in endemic regions. The Leishmania spp. evade host microbicidal mechanisms partially through virulence-associated proteins such as the major surface protease (MSP or GP63), to inactivate immune factors in the host environment. MSP is a metalloprotease encoded by a tandem array of genes belonging to three msp gene classes, whose mRNAs are differentially expressed in different life stages of the parasite. Like other cells, Leishmania spp. release small membrane-bound vesicles called exosomes into their environment. The purpose of this study was to detect MSP proteins in exosomal vesicles of Leishmania spp. protozoa. Methods Using mass spectrometry data we determined the profile of MSP class proteins released in L. infantum exosomes derived from promastigotes in their avirulent procyclic (logarithmic) stage and virulent stationary and metacyclic stages. MSP protein isoforms belonging to each of the three msp gene classes could be identified by unique peptides. Results Metacyclic promastigote exosomes contained the highest, and logarithmic exosomes had the lowest abundance of total MSP. Among the MSP classes, MSPC class had the greatest variety of isoforms, but was least abundant in all exosomes. Nonetheless, all MSP classes were present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes. Conclusions The data suggest the efficiency of exosome release may be more important than the identity of MSP isoform in determining the MSP content of Leishmania spp. exosomes. |
| first_indexed | 2024-12-12T19:36:32Z |
| format | Article |
| id | doaj.art-7da7d722aa9a40d2a62609a748e73ef5 |
| institution | Directory Open Access Journal |
| issn | 1756-3305 |
| language | English |
| last_indexed | 2024-12-12T19:36:32Z |
| publishDate | 2018-06-01 |
| publisher | BMC |
| record_format | Article |
| series | Parasites & Vectors |
| spelling | doaj.art-7da7d722aa9a40d2a62609a748e73ef52022-12-22T00:14:19ZengBMCParasites & Vectors1756-33052018-06-0111111010.1186/s13071-018-2937-yExtracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotesSkye Marshall0Patrick H. Kelly1Brajesh K. Singh2R. Marshall Pope3Peter Kim4Bayan Zhanbolat5Mary E. Wilson6Chaoqun Yao7Department of Biomedical Sciences and One Health Center for Zoonoses and Tropical Veterinary Medicine, Ross University School of Veterinary MedicineDepartment of Microbiology, University of IowaDepartment of Internal Medicine, University of IowaThe Proteomics Facility, University of IowaCarver College of Medicine, University of IowaDepartment of Internal Medicine, University of IowaDepartment of Microbiology, University of IowaDepartment of Biomedical Sciences and One Health Center for Zoonoses and Tropical Veterinary Medicine, Ross University School of Veterinary MedicineAbstract Background The Leishmania spp. protozoa are introduced into humans through a sand fly blood meal, depositing the infectious metacyclic promastigote form of the parasite into human skin. Parasites enter a variety of host cells, although a majority are found in macrophages where they replicate intracellularly during chronic leishmaniasis. Symptomatic leishmaniasis causes considerable human morbidity in endemic regions. The Leishmania spp. evade host microbicidal mechanisms partially through virulence-associated proteins such as the major surface protease (MSP or GP63), to inactivate immune factors in the host environment. MSP is a metalloprotease encoded by a tandem array of genes belonging to three msp gene classes, whose mRNAs are differentially expressed in different life stages of the parasite. Like other cells, Leishmania spp. release small membrane-bound vesicles called exosomes into their environment. The purpose of this study was to detect MSP proteins in exosomal vesicles of Leishmania spp. protozoa. Methods Using mass spectrometry data we determined the profile of MSP class proteins released in L. infantum exosomes derived from promastigotes in their avirulent procyclic (logarithmic) stage and virulent stationary and metacyclic stages. MSP protein isoforms belonging to each of the three msp gene classes could be identified by unique peptides. Results Metacyclic promastigote exosomes contained the highest, and logarithmic exosomes had the lowest abundance of total MSP. Among the MSP classes, MSPC class had the greatest variety of isoforms, but was least abundant in all exosomes. Nonetheless, all MSP classes were present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes. Conclusions The data suggest the efficiency of exosome release may be more important than the identity of MSP isoform in determining the MSP content of Leishmania spp. exosomes.http://link.springer.com/article/10.1186/s13071-018-2937-yLeishmaniaExosomeMajor surface proteaseVirulence factorsPromastigotes |
| spellingShingle | Skye Marshall Patrick H. Kelly Brajesh K. Singh R. Marshall Pope Peter Kim Bayan Zhanbolat Mary E. Wilson Chaoqun Yao Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes Parasites & Vectors Leishmania Exosome Major surface protease Virulence factors Promastigotes |
| title | Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes |
| title_full | Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes |
| title_fullStr | Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes |
| title_full_unstemmed | Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes |
| title_short | Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes |
| title_sort | extracellular release of virulence factor major surface protease via exosomes in leishmania infantum promastigotes |
| topic | Leishmania Exosome Major surface protease Virulence factors Promastigotes |
| url | http://link.springer.com/article/10.1186/s13071-018-2937-y |
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