Antibodies reacting with JCPyV_VP2 _167-15mer as a novel serological marker for JC polyomavirus infection

Abstract

BackgroundJC polyomavirus (JCPyV) is a widespread human polyomavirus that usually resides latently in its host, but can be reactivated under immune-compromised conditions potentially causing Progressive Multifocal Leukoencephalopathy (PML). Detection of antibodies against the major capsid protein VP1 currently is the main marker for assessment of infection with JCPyV.MethodsBased on a peptide microarray, peptide JCPyV_VP2_167-15mer was selected and a peptide ELISA was developed for detection of antibodies directed against this peptide. Epitope mapping and computational modelling was performed to further characterize this peptide. In a cohort of 204 healthy subjects it was investigated whether antibodies against JCPyV_VP2_167-15mer were correlated with VP1 serology or urinary viral load.ResultsEpitope mapping of peptide JCPyV_VP2_167-15mer showed that the minimal epitope consisted of L173PALTSQEI181 with amino acids P174, L176 and E180 being essential for antibody recognition. Computational analysis was used to predict that this epitope is located at an exposed domain of the VP2 capsid protein, readily accessible for immune recognition upon infection. No correlation could be observed with JCPyV VP1 antibody levels, or urinary viral load.ConclusionThis work indicates that specific antibodies against JCPyV_VP2_167-15mer might be considered as a novel serological marker for infection with JCPyV.Electronic supplementary materialThe online version of this article (doi:10.1186/1743-422X-11-174) contains supplementary material, which is available to authorized users.

Prevalence of antibodies against BKPyV subtype I and IV in kidney transplant recipients and in the general Czech population

“…Although these proteins are normally enclosed inside of virus particles, they can be recognized by the immune system during active infection to generate anti‐VP2/3 antibodies. The minor capsid proteins were previously shown to share conserved antigenic determinants in SV40, JCPyV, WU, and KI polyomaviruses, and antibodies recognizing these epitopes were found in experimental animal and normal human sera . Antigens containing a portion of disassembled material with minor capsid proteins could theoretically be well recognized by these antibodies in ELISA tests and could increase the background.…”

“…Altogether, these results indicate that in the doublereactive samples, both type-specific and type-common epitopes on the antibodies recognizing these epitopes were found in experimental animal and normal human sera. [34][35][36] Antigens containing a portion of disassembled material with minor capsid proteins could theoretically be well recognized by these antibodies in ELISA tests and could increase the background. VLPs prepared solely from VP1 should represent more specific antigens as shown in the present study.…”

Performance evaluation of 3 serodiagnostic peptide epitopes and the derived multi-epitope peptide OvNMP-48 for detection of Onchocerca volvulus infection

“…A second healthy control sample set was composed of 49 plasma samples from healthy individuals from Belgium. (Lagatie et al 2014a; Lagatie et al 2014b; Lagatie et al 2014c; Stuyver et al 2013; Van Loy et al 2013). Furthermore, different sets of plasma samples were obtained from Discovery Life Sciences, Inc. (Los Osos, USA), Bioreclamation IVT (Baltimore, USA), FR3, or Mayo Clinic (Jacksonville, USA).…”

2-Methyl-pentanoyl-carnitine (2-MPC): a urine biomarker for patent Ascaris lumbricoides infection

“…As a non-endemic control group, plasma and urine samples from Belgian healthy controls were included [37][38][39][40][41] . For all sample collections written informed consent was obtained from all individuals, and all samples were decoded and de-identified before they were provided for research purposes.…”