Guards of the great wall: bacterial lysozyme inhibitors

Callewaert, Lien; Herreweghe, J.M. Van; Vanderkelen, Lise; Leysen, S.; Voet, Arnout; Michiels, Chris W.

doi:10.1016/j.tim.2012.06.005

Cited by 90 publications

(112 citation statements)

References 58 publications

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“…Antibacterial activity of EWL is due to its ability to disrupt the bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) of the peptidgoglycan in bacterial cell walls (Callewaert et al, 2012;Lesnierowski & Kijowski, 2007). EWL is mostly active against Gram-positive bacteria, while Gramnegative bacteria are relatively resistant as the peptidoglycan layer of Gram-negative bacteria is protected by outer membrane compartment (Turner et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Purification of Egg White Lysozyme from Indonesian Kampung Chicken and Ducks

Wulandari

Fardiaz²,

Budiman³

et al. 2015

Med Pet

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Egg white lysozyme (EWL) has considerably a wide functional protein exhibiting antibacterial activity mainly against Gram-positive bacteria. The EWL is widely applied in food industry and is considerably safe. Despite its high potency, EWL of Indonesian poultry has never been studied and exploited. This study was aimed to purify EWL from two Indonesian poultry: kampung chicken and Cihateup duck, and compared to egg of commercial laying hens. The eggs in this study were obtained from field laboratory of Faculty of Animal Science, Bogor Agricultural University (IPB) and classified in AA quality based on the interior quality. First attempt to purify the EWL was performed by using ethanol precipitation yielding purified EWL which was still contaminated by other proteins, hence designated as partially purified EWL. Final concentrations of partially purified EWL of kampung chicken, commercial laying hens, and Cihateup duck were about 5800, 5400, and 5500 μg/mL, respectively. To confirm whether the use of ethanol in the purification affecting EWL antibacterial activities, the activities were examined against Staphylococcus aureus. It demonstrated that the partially purified EWL exhibited ability to inhibit S. aureus at 6 and 26 h suggesting that the method was feasible as it did not interfere EWL antibacterial activities. Yet, based on SDS-Page, purity was the issue in ethanol precipitation method. Further attempt using ion exchange chromatography at pH 10 successfully purified lysozyme as indicated by a single band corresponding to lysozyme size (~14 kD) free from bands of other proteins. Altogether, a single step of ion exchange chromatography is sufficient and promising to isolate EWL from Indonesian poultry for various industrial purposes.Key words: Indonesian poultry, lysozyme, egg, kampung chicken, Cihateup duck ABSTRAK Lisozim putih telur memiliki fungsi yang luas, salah satunya adalah memiliki aktivitas sebagai antibakteri terutama terhadap bakteri Gram positif. Lisozim dari putih telur �uga banyak diapli-. Lisozim dari putih telur �uga banyak diaplikasikan di industri pangan dan dinyatakan aman untuk pangan. Sampai saat ini lisozim dari putih telur yang berasal dari unggas lokal (Indonesia) belum dipela�ari dan dikembangkan. Tu�uan penelitian ini adalah melakukan purifikasi putih telur dari telur unggas lokal, yaitu ayam kampung dan itik Cihateup dibandingkan dengan telur ayam ras. Sampel telur yang didapatkan dari Laboratorium Lapang Fakultas Peternakan diklasifikasikan pada grade AA berdasarkan kualitas interior. Tahap pertama purifikasi lisozim putih telur dengan presipitasi etanol menghasilkan protein lain selain lisozim (purifikasi parsial). Konsentrasi lisozim putih telur hasil purifikasi parsial telur ayam kampung, ayam ras dan itik Cihateup masing-masing adalah 5800, 5400, dan 5500 ug/mL. Untuk melihat efek penggunaan etanol dalam proses purifikasi terhadap aktivitast antibakteri lisozim, kemampuan daya hambat lisozim terhadap Staphylococcus aureus telah dianalisis. Lisozim putih telur hasil pu...

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Section: Introductionmentioning

confidence: 99%

Purification of Egg White Lysozyme from Indonesian Kampung Chicken and Ducks

Wulandari

Fardiaz²,

Budiman³

et al. 2015

Med Pet

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“…Recently, it has been identified as one of the proteins with significant mycobactericidal activity from the pool of neutrophil granule proteins (18). Lysozyme inhibitors are important as they are essential for the survival of several pathogenic Gram-negative bacteria during infection in their animal hosts (19,20). In view of the antibacterial activity of lysozyme and because of the protection it endows at the cell surface, lysozyme inhibitors have been referred as the "guards of the great wall" (19) and thus are recognized as attractive targets for antibacterial drug design (21).…”

mentioning

confidence: 99%

Lipoprotein LprI of Mycobacterium tuberculosis Acts as a Lysozyme Inhibitor

Sethi¹,

Mahajan²,

Singh

et al. 2016

Journal of Biological Chemistry

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Mycobacterium tuberculosis, the causative agent of tuberculosis, is one of the most dreaded human pathogens that affect millions of lives worldwide (1). The inexplicable success of M. tuberculosis as a human pathogen relies on its ability to utilize a number of defense strategies to adapt its metabolism in response to a plethora of environmental challenges during the course of its pathogenic cycle (2, 3). Several of the components of its protein machinery have emerged as virulence factors with vital implications. Among these, lipoproteins play pivotal roles in several functions related to its virulence and host-pathogen interactions (4 -6). Genome analysis of mycobacteria indicated that the number of lipoproteins is much higher in the pathogenic mycobacteria in comparison with their non-pathogenic counterparts, and M. tuberculosis houses the highest number of lipoproteins.LprI is a novel lipoprotein that is exclusively present in pathogenic mycobacteria belonging to M. tuberculosis complex. The genomic location of the lprI gene is conserved among pathogenic mycobacteria where it has been identified as an operon partner of the glbN gene, which encodes truncated hemoglobin (HbN) 3 (7,8). The lprI gene is positioned adjacent to the glbN gene, separated through an intergenic distance of 58 nucleotides, and their co-transcription has been observed in Mycobacterium bovis (9), indicating that these two proteins may have functional correlation. The HbN of M. tuberculosis carries potent nitric oxide (NO) detoxification ability (8 -10) and is post-translationally modified by a glycan linkage that facilitates adherence and phagocytosis of cells during macrophage infection (11). The functional relevance of the co-occurrence of LprI with HbN in M. tuberculosis is unknown. Similar co-existence of a lipoprotein, LprG, along with Rv1410, which encodes a small molecule transporter, P55 (an operon conserved in M. tuberculosis complex), has also been observed in M. tuberculosis (12) where they function in a cooperative and synchronized manner. Because the HbN of M. tuberculosis plays a vital role in and is also involved in modulating host-pathogen interactions during intracellular infection of M. tuberculosis, it is likely that the glbN-lprI operon may also have some significant implications in the physiology of tubercle bacillus. LprI is an uncharacterized lipoprotein of M. tuberculosis complex; therefore, in the absence of any knowledge on LprI, its physiological function and implications of its co-existence with the HbN in M. tuberculosis are difficult to understand. To investigate the crucial implications of HbN in modulating the host-pathogen interactions and immune system of the host by providing aid in the better survival and sustenance of M. tuberculosis during intracellular infection, it is important to study the functionality of the LprI to understand functional implications of their co-occurrence in M. tuberculosis.In silico analysis unraveled that LprI carries a lysozyme-binding motif of the membrane-bound lysozyme in...

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“…The first of these to be identified was the E. coli Ivy (i.e., inhibitor of vertebrate lysozyme) protein (98) that inhibits only c-type lysozymes. Four other families of lysozyme inhibitors were subsequently identified; these differ in their localization (i.e., periplasmic [PliC] versus membrane bound [MliC]) and in their specificity for the different lysozyme types (i.e., c type, g type, or i type) (71).…”

Section: Discussionmentioning

confidence: 99%

“…The structural biology-derived prediction that both LipA and LipB were similar to bacterial lysozyme inhibitors also indicated that these proteins were likely localized to the periplasmic compartment in M. catarrhalis (71). To increase the likelihood of obtaining recombinant proteins that were folded properly, LipA and LipB were expressed as fusion proteins with a maltose-binding protein (MBP) that is secreted into the periplasm of E. coli.…”

Section: Fig 2 Growth Characteristics Of Wild-type M Catarrhalis Etsmentioning

confidence: 99%

A Moraxella catarrhalis Two-Component Signal Transduction System Necessary for Growth in Liquid Media Affects Production of Two Lysozyme Inhibitors

et al. 2015

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There are a paucity of data concerning gene products that could contribute to the ability of Moraxella catarrhalis to colonize the human nasopharynx. Inactivation of a gene (mesR) encoding a predicted response regulator of a two-component signal transduction system in M. catarrhalis yielded a mutant unable to grow in liquid media. This mesR mutant also exhibited increased sensitivity to certain stressors, including polymyxin B, SDS, and hydrogen peroxide. Inactivation of the gene (mesS) encoding the predicted cognate sensor (histidine) kinase yielded a mutant with the same inability to grow in liquid media as the mesR mutant. DNA microarray and real-time reverse transcriptase PCR analyses indicated that several genes previously shown to be involved in the ability of M. catarrhalis to persist in the chinchilla nasopharynx were upregulated in the mesR mutant. Two other open reading frames upregulated in the mesR mutant were shown to encode small proteins (LipA and LipB) that had amino acid sequence homology to bacterial adhesins and structural homology to bacterial lysozyme inhibitors. Inactivation of both lipA and lipB did not affect the ability of M. catarrhalis O35E to attach to a human bronchial epithelial cell line in vitro. Purified recombinant LipA and LipB fusion proteins were each shown to inhibit human lysozyme activity in vitro and in saliva. A lipA lipB deletion mutant was more sensitive than the wild-type parent strain to killing by human lysozyme in the presence of human apolactoferrin. This is the first report of the production of lysozyme inhibitors by M. catarrhalis. Moraxella catarrhalis is a Gram-negative coccobacillus that can cause disease in both the upper and lower respiratory tracts of humans (1). In infants and young children, this bacterium is a significant cause of acute otitis media (i.e., middle ear infection) (2-4). In adults, M. catarrhalis can cause infectious exacerbations of chronic obstructive pulmonary disease (COPD) (5-7) and is likely responsible for approximately 4 million exacerbations of COPD annually in the United States (6). The latter disease has global significance because it has been predicted that by 2020, COPD will become the third leading cause of death worldwide (reviewed in reference 8). In addition, M. catarrhalis can cause sinusitis, pneumonia, and, more rarely, bacteremia (1, 9).M. catarrhalis colonization of the human nasopharynx is apparently asymptomatic and, at least in infancy, can be correlated with an increased risk of otitis media (10). In this anatomic niche, M. catarrhalis likely forms a biofilm, together with the normal bacterial flora of the nasopharynx (11, 12). Once established in the nasopharynx, this bacterium can spread to the middle ear (causing otitis media) or to the lower respiratory tract (resulting in an infectious exacerbation of COPD). A number of putative M. catarrhalis colonization or virulence factors have been described in the past decade (13-20), but identification of those bacterial gene products that are truly essential for nasop...

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Guards of the great wall: bacterial lysozyme inhibitors

Cited by 90 publications

References 58 publications

Purification of Egg White Lysozyme from Indonesian Kampung Chicken and Ducks

Purification of Egg White Lysozyme from Indonesian Kampung Chicken and Ducks

Lipoprotein LprI of Mycobacterium tuberculosis Acts as a Lysozyme Inhibitor

A Moraxella catarrhalis Two-Component Signal Transduction System Necessary for Growth in Liquid Media Affects Production of Two Lysozyme Inhibitors

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