Evidence map›Paper›PMID 36445623›Full record

ArticleJournal, genetic engineering & biotechnology2022

Designing of novel chimeric PvpA-pMGA protein of Mycoplasma gallisepticum, applicable for indirect ELISA.

Farzaneh Pourkarimi Fatideh, Majid Esmaelizad, Mohammad Kargar, Majid Tebianian, Farshid Kafilzadeh

Open access · diamondAbstract read
In one paragraph

Article in Journal, genetic engineering & biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact, top 86% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 1 citations in OpenAlex.

  1. Assessment of the pathogenicity ofJournal of veterinary research · 2026
    Article
  2. Review
  3. Pathogenic mechanisms and vaccine development forFrontiers in microbiology · 2025
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Farzaneh Pourkarimi FatidehDepartment of Microbiology, Jahrom Branch, Islamic Azad University, Jahrom, Iran.
Majid EsmaelizadResearch and Development Department, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Karaj, Iran. m.esmaelizad@rvsri.ac.ir.ORCID http://orcid.org/0000-0001-8527-784X
Mohammad KargarDepartment of Microbiology, Jahrom Branch, Islamic Azad University, Jahrom, Iran.
Majid TebianianDepartment of Immunology, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Karaj, Iran.
Farshid KafilzadehDepartment of Microbiology, Jahrom Branch, Islamic Azad University, Jahrom, Iran.
Islamic Azad University, Jahrom Branch · IRRazi Vaccine and Serum Research Institute · IR

Funding

Razi Vaccine and Serum Research Institute 2-18-18-016-980385
6 · The paper itself

Abstract

backgroundMycoplasma gallisepticum is the primary agent of chronic respiratory disease in chickens creating important economic losses in poultry industry. pMGA and pvpA genes encode major surface proteins in M. gallisepticum containing pathogenic, antigenic, and immune evasion characteristics. The objective of the present study was to design, express, and purify the recombinant chimeric PvpA-pMGA protein from M.gallisepticum for using in serological diagnostic test.

methodsAntigenic regions of PvpA and pMGA proteins were predicted for designing chimeric pvpA-pMGA gene construct. The codon optimized sequence was cloned into the expression vector pET32a+ and transformed into the Escherichia coli strain BL21 (DE3). The pET32a-PvpA-pMGA recombinant plasmid was expressed and confirmed by SDS-PAGE and immunoblotting. PvpA-pMGA recombinant protein (20μg and 50μg), ts-11 vaccine strain, and S6 strain that formulated by montanide adjuvant and two control groups (PBS and adjuvant) were injected subcutaneously to six groups of chickens.

resultsHigh yield of protein was purified amount 138 mg/L by affinity batch formation method. Indirect ELISA showed the levels of antibodies in rPvpA-pMGA was significantly higher than ts-11 and S6 groups (p<0.05). The results indicated that antigen-specific response was successfully elicited by the rpMGA-PvpA in chickens. The result of the ELISA with sera collected from ts-11 and S6 groups showed that indirect PvpA-pMGA-ELISA is appropriate candidate for detection of specific antibodies against M. gallisepticum with 100% sensitivity and specificity.

conclusionsThe rPvpA-pMGA is a highly candidate immunogenic protein which induced high amount of humoral immune response. Novel rPvpA-pMGA protein could be useful for evaluation of antibody level in vaccinated poultry flocks.

Indexed as

Chimeric proteinELISAImmunogenicityMycoplasma gallisepticumPvpA-pMGARecombinant protein

Identifiers

PMID36445623
PMCPMC9708967
OpenAlexW4310239548

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.