ArticleVeterinary research communications2026
Recombinant P32 and B5R proteins of lumpy skin disease virus as candidate antigens for serodiagnostic applications.
Article in Veterinary research communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lumpy skin disease (LSD) virus poses a significant threat to bovine health and productivity in endemic regions, highlighting the need for reliable and standardized reagents for serological surveillance. However, the availability of standardized recombinant antigens for serological assays is limited in clinical settings. This study describes a bioinformatics-guided strategy for developing recombinant LSDV P32 and B5R antigens for serodiagnostic applications. Despite their notable immunogenicity, the P32 and B5R proteins, which are hydrophobic envelope proteins with transmembrane regions, present considerable challenges in terms of recombinant expression and purification. Initial attempts to express ectodomain-only constructs (P32Tr and B5RTr) using the pET-33b(+) system resulted in detectable proteins but faced significant challenges during purification. Guided by in silico predictions regarding solubility and aggregation propensity, the expression strategy was modified by employing a thioredoxin fusion system [pET-32a(+)], which facilitated expression and successful purification via Ni-NTA chromatography under denaturing conditions, followed by refolding. The purified recombinant proteins were confirmed using SDS-PAGE and immunoblotting. Preliminary indirect ELISA demonstrated the specific seroreactivity of both P32 and B5R proteins, confirming their antigenicity by showing reactivity with LSDV-positive sera without any cross-reactivity with sera from other bovine viruses. This study establishes a practical workflow to overcome the expression and purification challenges associated with aggregation-prone or hydrophobic proteins, thereby demonstrating the potential of recombinant P32 and B5R proteins as standardized biological reagents for use in serological assays.
Indexed as
Identifiers
41854938What OpenQuestion holds
Registered trials
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.