Lipopentapeptide induces a strong host humoral response and distinguishes Mycobacterium avium subsp. paratuberculosis from M. avium subsp. avium

Biet, Franck; Bay, Sylvie; Thibault, Virginie; Euphrasie, Daniel; Grayon, Maggy; Ganneau, Christelle; Lanotte, Philippe; Daffé, Mamadou; Gokhale, Rajesh S.; Etienne, Gilles; Reyrat, Jean‐Marc

doi:10.1016/j.vaccine.2007.10.059

Cited by 45 publications

(71 citation statements)

References 41 publications

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“…Heparinized whole blood was used for stimulation and IFN-γ response analyses. Approximately 6 h after sampling, 225 μL of whole blood was placed in 96-well plates (Falcon®) previously loaded with 25 μL of RPMI medium 1640 1× (Gibco® by Life Technologies™) as Nil antigen and 10 μg/mL of Purified Protein Derivative Avium (PPD-A 2500 Prionics Lelystad BV PPD-A); in addition for animal samples from the non-infected and M. bovis infected herds, wells had also been loaded with 10 μg/mL of Purified Protein Derivative Bovis (PPD-B 3000 Prionics Lelystad BV), 5 μg/mL of L5P synthesized chemically as previously described (Biet et al, 2008) and 5 μg/mL of Pokeweed mitogen (PWM) (Sigma-Aldrich) all diluted in RPMI. After stimulating for 24 h at 37°C and 5% CO 2 , whole blood was centrifuged at 1500 rpm, plasma was collected and frozen for IFN-γ cytokine quantification using an ELISA (Bovigam 1G ® Prionics).…”

Section: Methodsmentioning

confidence: 99%

“…Serology was performed with the IDEXX Map Ab Test (IDEXX Laboratories, Inc.) according to the manufacturer's instructions and the L5P humoral immune response was quantified as described previously (Biet et al, 2008).…”

Section: Methodsmentioning

confidence: 99%

“…In this study a cell wall lipopeptide antigen produced specifically by the Map subspecies: the lipopentapeptide L5P (Biet et al, 2008;Reyrat et al, 2009), was tested to recall CMI responses against Map. Previous studies have shown that L5P is abundant in lipid extracts from Map cells and differs greatly from glycopeptidolipids (GPLs), which are characteristic of the other M. avium complex (Mac) members (Barrow et al, 1995;Ripoll et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…Unlike GPL, L5P contains a peptide core which is not glycosylated due to the absence of a free hydroxyl group, and the fatty acid in the N-terminal domain of the molecule is shorter, saturated and not hydroxylated (Biet et al, 2008). This specific antigen has been synthesized chemically and evaluated in different studies for its potential use in serological assays to detect Map infection (Biet et al, 2008;Costanzo et al, 2012;Eckstein et al, 2006;Thirunavukkarasu et al, 2013;Verdier et al, 2013 …”

Section: Introductionmentioning

confidence: 99%

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Interferon gamma response to Mycobacterium avium subsp. paratuberculosis specific lipopentapeptide antigen L5P in cattle

Holbert

Branger

Souriau

et al. 2015

Research in Veterinary Science

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Interferon gamma response to Mycobacterium avium subsp. paratuberculosis specific lipopentapeptide antigen L5P in cattle

Holbert

Branger

Souriau

et al. 2015

Research in Veterinary Science

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“…Plates were then washed three times with PBS-0.05% Tween 20 (PBS/T) and were blocked for 1 h at 37°C with PBS/T containing 0.5% (wt/vol) gelatin (PBS/T/G). The sera tested have been described previously (32) and include a positive control from M. avium subsp. paratuberculosis-infected cattle, a negative control, and a set of sera obtained from ruminants naturally infected by M. avium subsp.…”

Section: Methodsmentioning

confidence: 99%

Novel Feature of Mycobacterium avium subsp. paratuberculosis, Highlighted by Characterization of the Heparin-Binding Hemagglutinin Adhesin

et al. 2013

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j Mycobacterium avium subsp. paratuberculosis comprises two genotypically defined groups, known as the cattle (C) and sheep (S) groups. Recent studies have reported phenotypic differences between M. avium subsp. paratuberculosis groups C and S, including growth rates, infectivity for macrophages, and iron metabolism. In this study, we investigated the genotypes and biological properties of the virulence factor heparin-binding hemagglutinin adhesin (HBHA) for both groups. In Mycobacterium tuberculosis, HBHA is a major adhesin involved in mycobacterium-host interactions and extrapulmonary dissemination of infection. To investigate HBHA in M. avium subsp. paratuberculosis, we studied hbhA polymorphisms by fragment analysis using the GeneMapper technology across a large collection of isolates genotyped by mycobacterial interspersed repetitive-unit-variable-number tandem-repeat (MIRU-VNTR) and IS900 restriction fragment length polymorphism (RFLP-IS900) analyses. Furthermore, we analyzed the structure-function relationships of recombinant HBHA proteins of types C and S by heparin-Sepharose chromatography and surface plasmon resonance (SPR) analyses. In silico analysis revealed two forms of HBHA, corresponding to the prototype genomes for the C and S types of M. avium subsp. paratuberculosis. This observation was confirmed using GeneMapper on 85 M. avium subsp. paratuberculosis strains, including 67 strains of type C and 18 strains of type S. We found that HBHAs from all type C strains contain a short C-terminal domain, while those of type S present a long C-terminal domain, similar to that produced by Mycobacterium avium subsp. avium. The purification of recombinant HBHA from M. avium subsp. paratuberculosis of both types by heparin-Sepharose chromatography highlighted a correlation between their affinities for heparin and the lengths of their C-terminal domains, which was confirmed by SPR analysis. Thus, types C and S of M. avium subsp. paratuberculosis may be distinguished by the types of HBHA they produce, which differ in size and adherence properties, thereby providing new evidence that strengthens the genotypic differences between the C and S types of M. avium subsp. paratuberculosis.

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Low cross‐reactivity of T‐cell responses against lipids from Mycobacterium bovis and M. avium paratuberculosis during natural infection

et al. 2009

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Although CD1 proteins are known to present mycobacterial lipid antigens to T cells, there is little understanding of the in vivo behavior of T cells restricted by CD1a, CD1b and CD1c, and the relative immunogenicity and immunodominance of individual lipids within the total array of lipids that comprise a bacterium. Because bovines express multiple CD1 proteins and are natural hosts of Mycobacterium bovis and Mycobacterium avium paratuberculosis (MAP), we used them as a new animal model of CD1 function. Here, we report the surprisingly divergent responses against lipids produced by these two pathogens during infection. Despite considerable overlap in lipid content, only three out of 69 animals cross-react with M. bovis and MAP total lipid preparations. The unidentified immunodominant compound of M. bovis is a hydrophilic compound, whereas the immunodominant lipid of MAP is presented by CD1b and was identified as glucose monomycolate (GMM). The preferential recognition of GMM antigen by MAP-infected cattle may be explained by the higher expression of GMM by MAP than by M. bovis. The bacterial species-specific nature of the CD1-restricted, adaptive T-cell response affects the approach to development of lipid based immunodiagnostic tests.

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Lipopentapeptide induces a strong host humoral response and distinguishes Mycobacterium avium subsp. paratuberculosis from M. avium subsp. avium

Cited by 45 publications

References 41 publications

Interferon gamma response to Mycobacterium avium subsp. paratuberculosis specific lipopentapeptide antigen L5P in cattle

Interferon gamma response to Mycobacterium avium subsp. paratuberculosis specific lipopentapeptide antigen L5P in cattle

Novel Feature of Mycobacterium avium subsp. paratuberculosis, Highlighted by Characterization of the Heparin-Binding Hemagglutinin Adhesin

Low cross‐reactivity of T‐cell responses against lipids from Mycobacterium bovis and M. avium paratuberculosis during natural infection

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