Passive immunization with a monoclonal IgM antibody specific for Strongyloides ratti HSP60 protects mice against challenge infection

Nouir, Nadia Ben; Piedavent, Melanie; Osterloh, Anke; Breloer, Minka

doi:10.1016/j.vaccine.2012.05.046

Cited by 22 publications

(20 citation statements)

References 21 publications

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“…The most recent study on S. japonicum [ 41 ] identified egg-derived HSP60 as a major parasite contributor of regulatory T-cell (Treg) induction among egg antigens [ 42 ]. Ben Nouir et al [ 43 ] used monoclonal IgM antibody specific for Strongyloides ratti HSP60 and revealed that vaccination with HSP60 conferred protection to infection in a murine model. In relation to our results, the presence of HSP60 among identified proteins may suggest that H .…”

Section: Discussionmentioning

confidence: 99%

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

et al. 2017

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BackgroundA wide range of molecules are used by tapeworm metacestodes to establish successful infection in the hostile environment of the host. Reports indicating the proteins in the cestode-host interactions are limited predominantly to taeniids, with no previous data available for non-taeniid species. A non-taeniid, Hymenolepis diminuta, represents one of the most important model species in cestode biology and exhibits an exceptional developmental plasticity in its life-cycle, which involves two phylogenetically distant hosts, arthropod and vertebrate.ResultsWe identified H. diminuta cysticercoid proteins that were recognized by sera of H. diminuta-infected rats using two-dimensional gel electrophoresis (2DE), 2D-immunoblotting, and LC-MS/MS mass spectrometry. Proteomic analysis of 42 antigenic spots revealed 70 proteins. The largest number belonged to structural proteins and to the heat-shock protein (HSP) family. These results show a number of the antigenic proteins of the cysticercoid stage, which were present already in the insect host prior to contact with the mammal host. These are the first parasite antigens that the mammal host encounters after the infection, therefore they may represent some of the molecules important in host-parasite interactions at the early stage of infection.ConclusionsThese results could help in understanding how H. diminuta and other cestodes adapt to their diverse and complex parasitic life-cycles and show universal molecules used among diverse groups of cestodes to escape the host response to infection.Electronic supplementary materialThe online version of this article (10.1186/s13071-017-2519-4) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

et al. 2017

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“…Additionally, Hsp60 act directly on antigen-presenting cells (APC) to link innate and adaptive immune responses [ 20 ]. Ben et al [ 21 ] found that immunization of mice with Strongyloides ratti Hsp60 (srHSP60) led to reduced numbers of migrating larvae, parasitic adults and larval output of S. ratti , and protected mice against nematode challenge infection. Moreover, immunization of female BALB/c mice with recombinant protein NP-M1-HSP60 induced immune responses, and protected mice from lethal influenza H7N9 virus challenge and significantly inhibited viral replication [ 22 ].…”

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confidence: 99%

Screening and Identification of Antigenic Proteins from the Hard Tick <i>Dermacentor silvarum</i> (Acari: Ixodidae)

Zhang

Cui

Zhang³

et al. 2015

Korean J Parasitol

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In order to explore tick proteins as potential targets for further developing vaccine against ticks, the total proteins of unfed female Dermacentor silvarum were screened with anti-D. silvarum serum produced from rabbits. The results of western blot showed that 3 antigenic proteins of about 100, 68, and 52 kDa were detected by polyclonal antibodies, which means that they probably have immunogenicity. Then, unfed female tick proteins were separated by 12% SDS-PAGE, and target proteins (100, 68, and 52 kDa) were cut and analyzed by LC-MS/MS, respectively. The comparative results of peptide sequences showed that they might be vitellogenin (Vg), heat shock protein 60 (Hsp60), and fructose-1, 6-bisphosphate aldolase (FBA), respectively. These data will lay the foundation for the further validation of antigenic proteins to prevent infestation and diseases transmitted by D. silvarum.

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“…It has been demonstrated that HSP60 represents a major component of Strongyloides ratti ESPs (excretory/secretory proteins) and presents functions as a target to the humoral and cellular immune response. Interestingly, the vaccination with alum-precipitated HSP60 or a passive immunization with a monoclonal anti-HSP60 IgM antibody, both specifics for Strongyloides ratti , conferred protection to mice against a challenge infection 20 21 .…”

Section: Discussionmentioning

confidence: 99%

Structural and functional characterization of a novel scFv anti-HSP60 of Strongyloides sp.

Levenhagen

Santos

Fujimura

et al. 2015

Sci Rep

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Phage display is a powerful technology that selects specific proteins or peptides to a target. We have used Phage Display to select scFv (single-chain variable fragment) clones from a combinatorial library against total proteins of Strongyloides venezuelensis. After scFv characterization, further analysis demonstrated that this recombinant fragment of antibody was able to bind to an S. venezuelensis antigenic fraction of ~65 kDa, present in the body periphery and digestive system of infective larvae (L3), as demonstrated by immunofluorescence. Mass spectrometry results followed by bioinformatics analysis showed that this antigenic fraction was a heat shock protein 60 (HSP60) of Strongyloides sp. The selected scFv was applied in serodiagnosis by immune complexes detection in serum samples from individuals with strongyloidiasis using a sandwich enzyme-linked immunosorbent assay (ELISA), showing sensitivity of 97.5% (86.84–99.94), specificity of 98.81 (93.54–99.97), positive likelihood ratio of 81.60 and an area under the curve of 0.9993 (0.9973–1.000). Our study provided a novel monoclonal scFv antibody fragment which specifically bound to HSP60 of Strongyloides sp. and was applied in the development of an innovative serodiagnosis method for the human strongyloidiasis.

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Passive immunization with a monoclonal IgM antibody specific for Strongyloides ratti HSP60 protects mice against challenge infection

Cited by 22 publications

References 21 publications

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

Screening and Identification of Antigenic Proteins from the Hard Tick <i>Dermacentor silvarum</i> (Acari: Ixodidae)

Structural and functional characterization of a novel scFv anti-HSP60 of Strongyloides sp.

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Passive immunization with a monoclonal IgM antibody specific for Strongyloides ratti HSP60 protects mice against challenge infection

Cited by 22 publications

References 21 publications

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

Screening and Identification of Antigenic Proteins from the Hard Tick &lt;i&gt;Dermacentor silvarum&lt;/i&gt; (Acari: Ixodidae)

Structural and functional characterization of a novel scFv anti-HSP60 of Strongyloides sp.

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Screening and Identification of Antigenic Proteins from the Hard Tick <i>Dermacentor silvarum</i> (Acari: Ixodidae)