The complete genome sequence of<i>Mycobacterium avium</i>subspecies<i>paratuberculosis</i>

Li, Lingling; Bannantine, John P.; Zhang, Qing; Amonsin, Alongkorn; May, Barbara; Alt, David P.; Banerji, Nilanjana; Kanjilal, Sagarika; Kapur, Vivek

doi:10.1073/pnas.0505662102

Cited by 407 publications

(386 citation statements)

References 69 publications

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“…The sequencing of the entire MAP genome (strain K-10) also significantly contributed to the precise detection and identification of MAP specific sequences (Li et al, 2005). With regard to the fact that various modifications of the PCR method are usually employed for MAP detection in milk, all possible "critical" steps will be analysed in detail in the following section.…”

Section: Map Detection Based On Molecular Techniquesmentioning

confidence: 99%

Detection methods for Mycobacterium avium subsp paratuberculosis in milk and milk products: a review

Slaná¹,

Paolicchi²,

Janštová³

et al. 2008

Vet. Med. - Czech

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Mycobacterium avium subsp. paratuberculosis (MAP) is the etiologic agent of paratuberculosis, a disease with considerable economic impact, principally on dairy cattle herds. Animals with paratuberculosis shed viable MAP especially in their milk, faeces and semen. MAP may have a role in the development of Crohn's disease in humans via the consumption of contaminated milk and milk products. The current methods of milk pasteurization are not sufficient to kill all MAP cells present in milk and MAP has been cultured from raw or pasteurized milk and isolated from cheese. The purpose of the present study was to review the different methods used for detection of MAP in milk and milk products. We analyze the current methods for direct or non direct identification of MAP and culture and molecular biology methods that can be applied to milk and milk products.

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Section: Map Detection Based On Molecular Techniquesmentioning

confidence: 99%

Detection methods for Mycobacterium avium subsp paratuberculosis in milk and milk products: a review

Slaná¹,

Paolicchi²,

Janštová³

et al. 2008

Vet. Med. - Czech

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“…17 MAP_1204 encodes a 244 amino acid protein with a calculated molecular weight of 25.4 kDa. Both proteins contain an Nterminal signal sequence predicted by the SignalP 4.1 server.…”

Section: Characteristics Of Map_1204 and Map_1272cmentioning

confidence: 99%

“…17 This is the same number of NlpC/P60 proteins annotated in M. tuberculosis 12 and Corynebacterium glutamicum genomes. 15 MAP_1203 shows increased expression, nearly 25-fold, when MAP is exposed to milk, 18 a hyperosmolar environment that triggers a more invasive form of the bacterium.…”

Section: Introductionmentioning

confidence: 97%

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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“…M. avium subsp. paratuberculosis [9], the bacterial agent of cattle Johne's disease, is also implicated in human Crohn's disease.…”

Section: Availability Of Microbial Genome Sequences Within Actinomycementioning

confidence: 99%

Defining mycobacteria: Shared and specific genome features for different lifestyles

Vissa

Sakamuri

et al. 2009

Indian J Microbiol

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During the last decade, the combination of rapid whole genome sequencing capabilities, application of genetic and computational tools, and establishment of model systems for the study of a range of species for a spectrum of biological questions has enhanced our cumulative knowledge of mycobacteria in terms of their growth properties and requirements. The adaption of the corynebacterial surrogate system has simplifi ed the study of cell wall biosynthetic machinery common to actinobacteria. Comparative genomics supported by experimentation reveals that superimposed on a common core of 'mycobacterial' gene set, pathogenic mycobacteria are endowed with multiple copies of several protein families that encode novel secretion and transport systems such as mce and esx; immunomodulators named PE/PPE proteins, and polyketide synthases for synthesis of complex lipids. The precise timing of expression, engagement and interactions involving one or more of these redundant proteins in their host environments likely play a role in the defi nition and differentiation of species and their disease phenotypes. Besides these, only a few species specifi c 'virulence' factors i.e., macromolecules have been discovered. Other subtleties may also arise from modifi cations of shared macromolecules. In contrast, to cope with the broad and changing growth conditions, their saprophytic relatives have larger genomes, in which the excess coding capacity is dedicated to transcriptional regulators, transporters for nutrients and toxic metabolites, biosynthesis of secondary metabolites and catabolic pathways. In this review, we present a sampling of the tools and techniques that are being implemented to tease apart aspects of physiology, phylogeny, ecology and pathology and illustrate the dominant genomic characteristics of representative species. The investigation of clinical isolates, natural disease states and discovery of new diagnostics, vaccines and drugs for existing and emerging mycobacterial diseases, particularly for multidrug resistant strains are the challenges in the coming decades.

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The complete genome sequence ofMycobacterium aviumsubspeciesparatuberculosis

Cited by 407 publications

References 69 publications

Detection methods for Mycobacterium avium subsp paratuberculosis in milk and milk products: a review

Detection methods for Mycobacterium avium subsp paratuberculosis in milk and milk products: a review

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

Defining mycobacteria: Shared and specific genome features for different lifestyles

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