Profiling Bovine Antibody Responses to
            <i>Mycobacterium avium</i>
            subsp.
            <i>paratuberculosis</i>
            Infection by Using Protein Arrays

Bannantine, John P.; Paustian, Michael L.; Waters, W. Ray; Stabel, Judith R.; Palmer, Mitchell V.; Li, Lingling; Kapur, Vivek

doi:10.1128/iai.00915-07

Cited by 31 publications

(32 citation statements)

References 59 publications

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“…paratuberculosis orthologs are present on the M. tuberculosis array but are not among the M. avium subsp. paratuberculosis proteins that have been previously analyzed on a protein array (2,4). Collectively, these data strengthened the hypothesis that the M. tuberculosis protein array might serve as a useful tool for screening over 1,800 additional candidate antigens for Johne's disease detection.…”

Section: Resultssupporting

confidence: 68%

“…Three antigens were identified for which antibodies were detected in calves by 70 days postinfection (4). Antigens during the later stages of Johne's disease were also identified in naturally infected cattle (2). However, these antigens are only the best of the subproteome represented on the protein array.…”

mentioning

confidence: 99%

“…paratuberculosis will be among the critical diagnostic tools in Johne's disease detection, especially in the early, subclinical stages of disease. Our group has previously used protein arrays to screen for seroreactive antigens during early (subclinical) and late (clinical) stages of Johne's disease (2). Animals appear healthy in the subclinical stage, but they shed small numbers of bacteria in their feces intermittently, thus serving as a transmission source for herd mates.…”

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confidence: 99%

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Identification of Novel Seroreactive Antigens in Johne's Disease Cattle by Using the Mycobacterium tuberculosis Protein Array

Bannantine

Campo

Randall

et al. 2017

Clin Vaccine Immunol

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Johne's disease, a chronic gastrointestinal inflammatory disease caused by Mycobacterium avium subspecies paratuberculosis, is endemic in dairy cattle and other ruminants worldwide and remains a challenge to diagnose using traditional serological methods. Given the close phylogenetic relationship between M. avium subsp. paratuberculosis and the human pathogen Mycobacterium tuberculosis, here, we applied a whole-proteome M. tuberculosis protein array to identify seroreactive and diagnostic M. avium subsp. paratuberculosis antigens. A genome-scale pairwise analysis of amino acid identity levels between orthologous proteins in M. avium subsp. paratuberculosis and M. tuberculosis showed an average of 62% identity, with more than half the orthologous proteins sharing Ͼ75% identity. Analysis of the M. tuberculosis protein array probed with sera from M. avium subsp. paratuberculosisinfected cattle showed antibody binding to 729 M. tuberculosis proteins, with 58% of them having Ն70% identity to M. avium subsp. paratuberculosis orthologs. The results showed that only 4 of the top 40 seroreactive M. tuberculosis antigens were orthologs of previously reported M. avium subsp. paratuberculosis antigens, revealing the existence of a large number of previously unrecognized candidate diagnostic antigens. Enzyme-linked immunosorbent assay (ELISA) testing of 20 M. avium subsp. paratuberculosis recombinant proteins, representing reactive and nonreactive M. tuberculosis orthologs, further confirmed that the M. tuberculosis array has utility as a screening tool for identifying candidate antigens for Johne's disease diagnostics. Additional ELISA testing of field serum samples collected from dairy herds around the United States revealed that MAP2942c had the strongest seroreactivity with Johne's disease-positive samples. Collectively, our studies have considerably expanded the number of candidate M. avium subsp. paratuberculosis proteins with potential utility in the next generation of rationally designed Johne's disease diagnostic assays.

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Section: Resultssupporting

confidence: 68%

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confidence: 99%

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confidence: 99%

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Identification of Novel Seroreactive Antigens in Johne's Disease Cattle by Using the Mycobacterium tuberculosis Protein Array

Bannantine

Campo

Randall

et al. 2017

Clin Vaccine Immunol

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“…37 Such a resource makes it possible to analyze the activities of proteins in cell growth, maintenance, regulation, survival, and pathogenesis. Additionally, this resource can provide reagents for diagnostics 38,39 and functional proteomic experiments, including both the structural studies described herein as well as defining proteinprotein interactions. Finally, tools such as this repository build on genomic information by aiding in the functional annotation of the hundreds of hypothetical proteins.…”

Section: Discussionmentioning

confidence: 99%

NlpC/P60 domain‐containing proteins of Mycobacterium avium subspecies paratuberculosis that differentially bind and hydrolyze peptidoglycan

et al. 2016

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A subset of proteins containing NlpC/P60 domains are bacterial peptidoglycan hydrolases that cleave noncanonical peptide linkages and contribute to cell wall remodeling as well as cell separation during late stages of division. Some of these proteins have been shown to cleave peptidoglycan in Mycobacterium tuberculosis and play a role in Mycobacterium marinum virulence of zebra fish; however, there are still significant knowledge gaps concerning the molecular function of these proteins in Mycobacterium avium subspecies paratuberculosis (MAP). The MAP genome sequence encodes five NlpC/P60 domain-containing proteins. We describe atomic resolution crystal structures of two such MAP proteins, MAP_1272c and MAP_1204. These crystal structures, combined with functional assays to measure peptidoglycan cleavage activity, led to the observation that MAP_1272c does not have a functional catalytic core for peptidoglycan hydrolysis. Furthermore, the structure and sequence of MAP_1272c demonstrate that the catalytic residues normally required for hydrolysis are absent, and the protein does not bind peptidoglycan as efficiently as MAP_1204. While the NlpC/P60 catalytic triad is present in MAP_1204, changing the catalytic cysteine-155 residue to a serine significantly diminished catalytic activity, but did not affect binding to peptidoglycan. Collectively, these findings suggest a broader functional repertoire for NlpC/P60 domain-containing proteins than simply hydrolases. Keywords: Mycobacterium; Johne's disease; crystal structure; peptidoglycan; proteins; antigens; paratuberculosis Additional Supporting Information may be found in the online version of this article.Importance: Johne's disease in ruminant livestock is caused by the bacterium Mycobacterium avium subspecies paratuberculosis. This research describes the functional aspects of two proteins that show promise in a subunit vaccine for Johne's disease. Through crystal structure determination and amino acid modification, we demonstrate that although both proteins have a similar structure, one of them lacked hydrolytic activity on peptidoglycan. We show that a specific amino acid is likely responsible for this lack of hydrolytic activity.

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“…6). The NlpC recombinant protein was next tested along with 9 other proteins ranked among the most immunogenic, yet with the least background reactivity as determined by a previous protein array study (3). These included proteins encoded by MAP0857c, MAP0865, MAP0900, MAP2077c, MAP2116c, MAP3155c, MAP3735c, MAP3817c, and MAP4014.…”

Section: Resultsmentioning

confidence: 99%

MAP1272c Encodes an NlpC/P60 Protein, an Antigen Detected in Cattle with Johne's Disease

Bannantine

Lingle

Stabel

et al. 2012

Clin. Vaccine Immunol.

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The protein encoded by MAP1272c has been shown to be an antigen of Mycobacterium avium subsp. paratuberculosis that contains an NlpC/P60 superfamily domain found in lipoproteins or integral membrane proteins. Proteins containing this domain have diverse enzymatic functions that include peptidases, amidases, and acetyltransferases. The NlpC protein was examined in comparison to over 100 recombinant proteins and showed the strongest antigenicity when analyzed with sera from cattle with Johne's disease. To further localize the immunogenicity of NlpC, recombinant proteins representing defined regions were expressed and evaluated with sera from cattle with Johne's disease. The region from amino acids 74 to 279 was shown to be the most immunogenic. This fragment was also evaluated against a commercially available enzyme-linked immunosorbent assay (ELISA). Two monoclonal antibodies were produced in mice immunized with the full-length protein, and each recognized a distinct epitope. These antibodies cross-reacted with proteins from other mycobacterial species and demonstrated variable sizes of the proteins expressed from these subspecies. Both antibodies were further analyzed, and their interaction with MAP1272c and MAP1204 was characterized by a solution-based, luminescent binding assay. These tools provide additional means to study a strong antigen of M. avium subsp. paratuberculosis.

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Profiling Bovine Antibody Responses to Mycobacterium avium subsp. paratuberculosis Infection by Using Protein Arrays

Cited by 31 publications

References 59 publications

Identification of Novel Seroreactive Antigens in Johne's Disease Cattle by Using the Mycobacterium tuberculosis Protein Array

Identification of Novel Seroreactive Antigens in Johne's Disease Cattle by Using the Mycobacterium tuberculosis Protein Array

NlpC/P60 domain‐containing proteins of Mycobacterium avium subspecies paratuberculosis that differentially bind and hydrolyze peptidoglycan

MAP1272c Encodes an NlpC/P60 Protein, an Antigen Detected in Cattle with Johne's Disease

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