Preheat Treatment for Mycobacterium tuberculosis Hsp16.3: Correlation between a Structural Phase Change at 60°C and a Dramatic Increase in Chaperone-like Activity

Mao, Qilong; Ke, Danxia; Feng, Xiuguang; Chang, Zengyi

doi:10.1006/bbrc.2001.5074

Cited by 30 publications

(28 citation statements)

References 19 publications

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“…It is a stress protein induced by hypoxic culture conditions. Other evidence (11,14,23,31) has led to the proposition that HspX has a central role in the viability of the bacilli during latent, asymptomatic infections in humans and in a mouse model of TB. In contrast, its role in bovine TB has been not studied.…”

Section: Discussionmentioning

confidence: 99%

Identification of Novel Mycobacterium bovis Antigens by Dissection of Crude Protein Fractions

Meikle¹,

Alito²,

Llera

et al. 2009

Clin Vaccine Immunol

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Culture filtrate and cell extracts from Mycobacterium bovis cultures contain molecules which could promote protective immunity to tuberculosis in animals. Different protein fractions of M. bovis cultures were obtained by elution electrophoresis and were tested in experimentally infected cattle. The fractions that elicited gamma interferon (IFN-␥) responses were resolved by two-dimensional gel electrophoresis, and individual proteins were identified by matrix-assisted laser desorption ionization-time of flight mass spectrometry. The open reading frames were cloned, expressed as their recombinant forms, and retested with naturally and experimentally infected animals. Eleven protein fractions were highly reactive, from which the Rv1636, HspX, Rv0138, Rv2524, EsxI, and Rv3740 recombinant proteins were obtained. EsxI and HspX were the antigens most recognized by the IFN-␥ release assay. In summary, a proteomic approach allowed the identification of novel antigens useful for the diagnosis of bovine tuberculosis.Infection and disease with Mycobacterium bovis, the causative organism of bovine tuberculosis (TB), is an important health problem in cattle and other animal species. The disease presents a major barrier to animal-related trade and production, causing significant losses to farming economies worldwide. Furthermore, bovine TB has serious zoonotic implications, especially in developing regions. In North and South America, there are 420 million cattle, half of which are in countries with an incidence of bovine TB higher than 1% (13). The disease control programs carried out in most countries are based on a test and removal strategy utilizing the tuberculin skin test (TST) with purified protein derivative (PPD) (4). Accurate detection using the TST and removal of infected cattle form the base of control strategies for bovine TB. It is widely recognized that tests for cell-mediated immunity are far more sensitive than antibody tests in detecting bovine TB (38). Disease control based on the use of PPD can be facilitated by using the gamma interferon (IFN-␥) test for bovine TB (39). The PPDs are obtained by acid precipitation from heat-killed cultures of M. bovis (PPD-B) and Mycobacterium avium (PPD-A) and are poorly defined (27), containing many proteins, lipids, and sugars. Many of these compounds are shared by different mycobacterial species or even with other bacteria (22). The detection of false positives has been a significant part of the economic cost, particularly in areas where there is a relatively low incidence of the disease (28), and thus, there is an urgent need for more specific reagents for the diagnosis of M. bovis infection.Many mycobacterial proteins have been isolated, and bovine T-cell epitopes have been characterized for several of them (2, 9, 26, 30, 32). Immunodominant peptides from M. tuberculosis Rv3873, Rv3879c, Rv3019c, Rv0288, ESAT-6, and CFP-10 genes were described as good T-cell inducers, and the diagnostic potential of a cocktail composed of these dominant peptides was demonstrated using...

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Section: Discussionmentioning

confidence: 99%

Identification of Novel Mycobacterium bovis Antigens by Dissection of Crude Protein Fractions

Meikle¹,

Alito²,

Llera

et al. 2009

Clin Vaccine Immunol

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“…The upstream gene MAP0483 encodes a transcription-regulatory protein in M. tuberculosis. Another transcription protein, encoded by MAP1695c, acts as a cochaperone in M. tuberculosis (19,27). The upstream gene is for Hsp18, a stress protein induced by anoxia.…”

Section: Discussionmentioning

confidence: 99%

The Ability ofMycobacterium aviumsubsp.paratuberculosisTo Enter Bovine Epithelial Cells Is Influenced by Preexposure to a Hyperosmolar Environment and Intracellular Passage in Bovine Mammary Epithelial Cells

et al. 2006

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Mycobacterium avium subsp. paratuberculosis is the cause of Johne's disease in cattle and other ruminants. M. avium subsp. paratuberculosis infection of the bovine host is not well understood; however, it is assumed that crossing the bovine intestinal mucosa is important in order for M. avium subsp. paratuberculosis to establish infection. To examine the ability of M. avium subsp. paratuberculosis to infect bovine epithelial cells in vitro, Madin-Darby bovine kidney (MDBK) epithelial cells were exposed to M. avium subsp. paratuberculosis. It was observed that bacteria can establish infection and replicate within MDBK cells. M. avium subsp. paratuberculosis also has been reported to infect mammary tissue and milk, and we showed that M. avium subsp. paratuberculosis infects bovine mammary epithelial cells (MAC-T cell line). Using polarized MAC-T cell monolayers, it was also determined that M. avium subsp. paratuberculosis crosses apical and basolateral surfaces with approximately the same degree of efficiency. Because M. avium subsp. paratuberculosis can be delivered to the naïve host by milk, it was investigated whether incubation of M. avium subsp. paratuberculosis with milk has an effect on invasion of MDBK cells. M. avium subsp. paratuberculosis exposed to milk entered epithelial cells with greater efficiency than M. avium subsp. paratuberculosis exposed to broth medium or water (P < 0.01). Growth of M. avium subsp. paratuberculosis within MAC-T cells also resulted in augmented ability to subsequently infect bovine MDBK cells (P < 0.001). Microarray analysis of intracellular M. avium subsp. paratuberculosis RNA indicates the increased transcription of genes which might be associated with an invasive phenotype.Mycobacterium avium subsp. paratuberculosis is the etiologic agent of Johne's disease in cattle and other ruminants. It is assumed that M. avium subsp. paratuberculosis infects the young calf by crossing the intestinal barrier. Previous work (3, 26) has indicated that the interaction of M. avium subsp. paratuberculosis with bovine epithelial cells is a complex process which might involve participation of several bacterial and host factors. For example, it has been reported that both in calves and in mice, challenge by the gastrointestinal route results in M. avium subsp. paratuberculosis infecting M cells in the Peyer's patches (23,26). Recently, Secott and colleagues have suggested that the invasion of the intestinal mucosa by M. avium subsp. paratuberculosis is secondary to the binding to fibronectin (26). In addition, Bannantine and colleagues demonstrated a role for a 35-kDa M. avium subsp. paratuberculosis protein in the invasion of cultured bovine epithelial cells (5). The 35-kDa protein is exposed in the outer layer of M. avium subsp. paratuberculosis and has also been associated with Mycobacterium avium invasion of human intestinal cells (22).After M. avium subsp. paratuberculosis crosses the intestinal mucosa, the infection spreads to other organs, leading to the advanced stages of disease. Sever...

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“…Glycine 114 is housed in the conserved G-X-L motif of a short loop joining b-strands 8 and 9, but knowing this fails to show how glycine modifi cation affects chaperone activity and not oligomerization [90]. Mutation of leucine 122 in M. tuberculosis Hsp16.3, located in the conserved motif GVLTVTV, and the equivalent leucine 116 in B. japonicum HspH, undermines chaperone function in both proteins, although the effect on oligomerization is greater for HspH than Hsp16.3 [90,95]. Leucine 122 of Hsp16.3 corresponds to leucine 129 of M. jannaschii Hsp16.5, and is located at the start of b-strand 9 between b-strands 4 and 5, close to a potential hydrophobic motif of IIL at positions 67-69.…”

Section: Shsp Crystallization and The A-crystallin Domainmentioning

confidence: 99%

Small heat shock proteins: molecular structure and chaperone function

Sun

MacRae

2005

Cell. Mol. Life Sci.

439

352

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Small heat shock proteins (sHSPs) associate with nuclei, cytoskeleton and membranes, and as molecular chaperones they bind partially denatured proteins, thereby preventing irreversible protein aggregation during stress. sHSP monomers consist of a conserved alpha-crystallin domain of approximately 90 amino acid residues, bordered by variable amino- and carboxy-terminal extensions. The sHSPs undergo dynamic assembly into mono- and poly-disperse oligomers where the rate of disassembly affects chaperoning. The alpha-crystallin domain contains several beta-strands organized into two beta-sheets responsible for dimer formation, the basic building block of most sHSPS. The amino-terminal extension modulates oligomerization, subunit dynamics and substrate binding, whereas the flexible carboxy-terminal extension promotes solubility, chaperoning and oligomerization, the latter by inter-subunit linkage. Crystallization studies have revealed sHSP structure and function. Additionally, site-directed mutagenesis, biophysical investigations, functional studies and the discovery of relationships between mutated sHSPs and diseases have illuminated the role of sHSP within cells.

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Preheat Treatment for Mycobacterium tuberculosis Hsp16.3: Correlation between a Structural Phase Change at 60°C and a Dramatic Increase in Chaperone-like Activity

Cited by 30 publications

References 19 publications

Identification of Novel Mycobacterium bovis Antigens by Dissection of Crude Protein Fractions

Identification of Novel Mycobacterium bovis Antigens by Dissection of Crude Protein Fractions

The Ability ofMycobacterium aviumsubsp.paratuberculosisTo Enter Bovine Epithelial Cells Is Influenced by Preexposure to a Hyperosmolar Environment and Intracellular Passage in Bovine Mammary Epithelial Cells

Small heat shock proteins: molecular structure and chaperone function

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