B-cell linear epitopes mapping of antigen-5 allergen from Polybia paulista wasp venom

The social wasp Polybia paulista (Hymenoptera, Vespidae) is highly aggressive, being responsible for many medical occurrences. One of the most allergenic components of this venom is Antigen 5 (Poly p 5). The possible modulation of the in vitro immune response induced by antigen 5 from P. paulista venom, expressed recombinantly (rPoly p 5), on BALB/c mice peritoneal macrophages, activated or not with LPS, was assessed. Here, we analyzed cell viability changes, expression of the phosphorylated form of p65 NF-κB subunit, nitric oxide (NO), proinflammatory cytokines production, and co-stimulatory molecules (CD80, CD86). The results suggest that rPoly p 5 does not affect NO production nor the expression of co-stimulatory molecules in mouse peritoneal macrophages. On the other hand, rPoly p 5 induced an increase in IL-1β production in non-activated macrophages and a reduction in the production of TNF-α and MCP-1 cytokines in activated macrophages. rPoly p 5 decreased the in vitro production of the phosphorylated p65 NF-κB subunit in non-activated macrophages. These findings suggest an essential role of this allergen in the polarization of functional M2 macrophage phenotypes, when analyzed in previously activated macrophages. Further investigations, mainly in in vivo studies, should be conducted to elucidate Polybia paulista Ag5 biological role in the macrophage functional profile modulation.

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Mapping and characterization of B cell linear epitopes in the conservative regions of hepatitis C virus envelope glycoproteins

Journal of Viral Hepatitis ◽

10.1046/j.1365-2893.2002.00358.x ◽

2002 ◽

Vol 9 (3) ◽

pp. 174-182 ◽

Cited By ~ 13

Author(s):

L. V. Olenina ◽

L. I. Nikolaeva ◽

B. N. Sobolev ◽

N. P. Blokhina ◽

A. I. Archakov ◽

...

Keyword(s):

Hepatitis C Virus ◽

Hepatitis C ◽

B Cell ◽

Envelope Glycoproteins ◽

Virus Envelope ◽

Linear Epitopes

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B-Cell Linear Epitopes in the Conservative Regions of Hepatitis C Virus Envelope Glycoproteins

Peptides: The Wave of the Future ◽

10.1007/978-94-010-0464-0_482 ◽

2001 ◽

pp. 1031-1032

Author(s):

Ekaterina F. Kolesanova ◽

Ludmila V. Olenina ◽

Boris N. Sobolev ◽

Ludmila I. Nikolaeva ◽

Alexander I. Archakov

Keyword(s):

Hepatitis C Virus ◽

Hepatitis C ◽

B Cell ◽

Envelope Glycoproteins ◽

Virus Envelope ◽

Linear Epitopes

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Identification of B-cell linear epitopes in domains 1–3 of pyolysin of Trueperella pyogenes using polyclonal antibodies

Veterinary Microbiology ◽

10.1016/j.vetmic.2017.08.018 ◽

2017 ◽

Vol 210 ◽

pp. 24-31 ◽

Cited By ~ 6

Author(s):

Lingxiao Yang ◽

Yue Zhang ◽

Haili Wang ◽

Bo Ma ◽

Li Xu ◽

...

Keyword(s):

B Cell ◽

Polyclonal Antibodies ◽

Trueperella Pyogenes ◽

Linear Epitopes

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Identification of specific B cell linear epitopes of mycoplasma hyorhinis P37 protein using monoclonal antibodies against baculovirus-expressed P37 protein

BMC Microbiology ◽

10.1186/s12866-019-1614-4 ◽

2019 ◽

Vol 19 (1) ◽

Cited By ~ 1

Author(s):

Hongzhen Zhu ◽

Yanwu Wei ◽

Liping Huang ◽

Dan Liu ◽

Yongxing Xie ◽

...

Keyword(s):

Amino Acids ◽

Monoclonal Antibodies ◽

B Cell ◽

Etiologic Agent ◽

Mycoplasma Hyorhinis ◽

Humoral Immune ◽

Humoral Immune Responses ◽

Precise Analysis ◽

Linear Epitopes ◽

Specific Antigens

Abstract Background Mycoplasma hyorhinis (Mhr) is the etiologic agent of lameness and polyserositis in swine. P37 is a membrane protein of Mhr that may be an important immunogen and is a potential target for diagnostic development. However, there is little information concerning Mhr P37 protein epitopes. A precise analysis of the P37 protein epitopes should extend our understanding of the antigenic composition of the P37 protein and the humoral immune responses to Mhr infection. Investigating the epitopes of Mhr P37 will help to establish a detection method for Mhr in tissue and provide an effective tool for detecting Mhr infection. Results Western blot and indirect immunofluorescence assays (IFA) confirmed that the expressed P37 protein was recognized by Mhr-positive porcine and mouse sera. Furthermore, the P37 protein was purified using affinity chromatography and used to immunize mice for hybridoma cell fusion. Four monoclonal antibodies (mAbs) found to be positive for Mhr were detected in infected lung tissue. A panel of truncated P37 proteins was used to identify the minimal B cell linear epitopes of the protein based on these mAbs. The core epitope was determined to be 206KIKKAWNDKDWNTFRNF222. Conclusions In this study, we identified 17 critical amino acids that determine the epitope of the P37 protein of Mhr. This study identified mAbs that could provide useful tools for investigating the Mhr P37 antigenic core epitope (amino acids 206–222) and detecting Mhr-specific antigens in infected tissue.

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A novel cDNA from Drosophila encoding a protein with similarity to mammalian cysteine-rich secretory proteins, wasp venom antigen 5, and plant group 1 pathogenesis-related proteins

Gene ◽

10.1016/s0378-1119(97)00010-3 ◽

1997 ◽

Vol 191 (2) ◽

pp. 135-141 ◽

Cited By ~ 38

Author(s):

Michael C Schreiber ◽

J.Colleen Karlo ◽

Gae E Kovalick

Keyword(s):

Secretory Proteins ◽

Wasp Venom ◽

Pathogenesis Related Proteins ◽

Plant Group ◽

Pathogenesis Related ◽

Related Proteins ◽

Antigen 5 ◽

Group 1

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In SilicoPrediction of T and B Cell Epitopes of Der f 25 inDermatophagoides farinae

International Journal of Genomics ◽

10.1155/2014/483905 ◽

2014 ◽

Vol 2014 ◽

pp. 1-10 ◽

Cited By ~ 14

Author(s):

Xiaohong Li ◽

Hai-Wei Yang ◽

Hao Chen ◽

Jing Wu ◽

Yehai Liu ◽

...

Keyword(s):

T Cell ◽

B Cell ◽

Triosephosphate Isomerase ◽

Allergic Diseases ◽

Major Allergen ◽

House Dust Mites ◽

T Cell Epitopes ◽

B Cell Epitopes ◽

Physiochemical Properties ◽

Linear Epitopes

The house dust mites are major sources of indoor allergens for humans, which induce asthma, rhinitis, dermatitis, and other allergic diseases. Der f 25 is a triosephosphate isomerase, representing the major allergen identified inDermatophagoides farinae. The objective of this study was to predict the B and T cell epitopes of Der f 25. In the present study, we analyzed the physiochemical properties, function motifs and domains, and structural-based detailed features of Der f 25 and predicted the B cell linear epitopes of Der f 25 by DNAStar protean system, BPAP, and BepiPred 1.0 server and the T cell epitopes by NetMHCIIpan-3.0 and NetMHCII-2.2. As a result, the sequence and structure analysis identified that Der f 25 belongs to the triosephosphate isomerase family and exhibited a triosephosphate isomerase pattern (PS001371). Eight B cell epitopes (11–18, 30–35, 71–77, 99–107, 132–138, 173–187, 193–197, and 211–224) and five T cell epitopes including 26–34, 38–54, 66–74, 142–151, and 239–247 were predicted in this study. These results can be used to benefit allergen immunotherapies and reduce the frequency of mite allergic reactions.

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Identification of Mycoplasma hyorhinis P37 protein-specific B cell linear epitopes using monoclonal antibodies against baculovirus-expressed P37 protein

10.21203/rs.2.9644/v1 ◽

2019 ◽

Author(s):

Hongzhen Zhu ◽

Yanwu Wei ◽

Liping Huang ◽

Dan Liu ◽

Yongxing Xie ◽

...

Keyword(s):

Monoclonal Antibodies ◽

B Cell ◽

Critical Role ◽

Diagnostic Techniques ◽

Etiologic Agent ◽

Antigenic Structure ◽

Mycoplasma Hyorhinis ◽

Linear Epitopes ◽

Baculovirus System ◽

And Function

Abstract Background Mycoplasma hyorhinis (Mhr) is the etiologic agent of lameness and polyserositis in swine. Mhr P37 is a membrane protein that may play a critical role in immunity. It is a potential target for diagnostic development, but there is little information concerning its B cell epitopes. To investigate the epitopes of Mhr P37, a recombinant protein was developed in a baculovirus system using monoclonal antibodies (mAbs) prepared against P37 protein. Results Western blot and indirect immunofluorescence assays (IFA) confirmed that the expressed P37 protein was recognized by Mhr-positive porcine and mouse sera. Furthermore, the P37 protein was purified using affinity chromatography and used to immunize mice for hybridoma cell fusion. Four mAbs were found to be positive for Mhr. A panel of truncated P37 proteins was used to identify the minimal B cell linear epitopes of the protein based on these mAbs. The core epitope was determined to be 206KIKKAWNDKDWNTFRNF222. Conclusions This study identified mAbs that could provide useful tools for investigating the antigenic structure and function of the Mhr P37 protein as well as its application to diagnostic techniques.

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