Search Results - "Lovering, Andrew L"

Structural Perspective of Peptidoglycan Biosynthesis and Assembly by Lovering, Andrew L, Safadi, Susan S, Strynadka, Natalie C.J

“…The peptidoglycan biosynthetic pathway is a critical process in the bacterial cell and is exploited as a target for the design of antibiotics. This pathway…”
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Two-site recognition of Staphylococcus aureus peptidoglycan by lysostaphin SH3b by Gonzalez-Delgado, Luz S., Walters-Morgan, Hannah, Salamaga, Bartłomiej, Robertson, Angus J., Hounslow, Andrea M., Jagielska, Elżbieta, Sabała, Izabela, Williamson, Mike P., Lovering, Andrew L., Mesnage, Stéphane

“…Lysostaphin is a bacteriolytic enzyme targeting peptidoglycan, the essential component of the bacterial cell envelope. It displays a very potent and specific…”
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Asymmetric peptidoglycan editing generates cell curvature in Bdellovibrio predatory bacteria by Banks, Emma J., Valdivia-Delgado, Mauricio, Biboy, Jacob, Wilson, Amber, Cadby, Ian T., Vollmer, Waldemar, Lambert, Carey, Lovering, Andrew L., Sockett, R. Elizabeth

“…Peptidoglycan hydrolases contribute to the generation of helical cell shape in Campylobacter and Helicobacter bacteria, while cytoskeletal or periskeletal…”
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A lysozyme with altered substrate specificity facilitates prey cell exit by the periplasmic predator Bdellovibrio bacteriovorus by Harding, Christopher J., Huwiler, Simona G., Somers, Hannah, Lambert, Carey, Ray, Luke J., Till, Rob, Taylor, Georgina, Moynihan, Patrick J., Sockett, R. Elizabeth, Lovering, Andrew L.

“…Lysozymes are among the best-characterized enzymes, acting upon the cell wall substrate peptidoglycan. Here, examining the invasive bacterial periplasmic…”
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Prey killing without invasion by Bdellovibrio bacteriovorus defective for a MIDAS-family adhesin by Tyson, Jess, Radford, Paul, Lambert, Carey, Till, Rob, Huwiler, Simona G., Lovering, Andrew L., Elizabeth Sockett, R.

“…The bacterium Bdellovibrio bacteriovorus is a predator of other Gram-negative bacteria. The predator invades the prey’s periplasm and modifies the prey’s cell…”
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Structural basis for activation of a diguanylate cyclase required for bacterial predation in Bdellovibrio by Meek, Richard W., Cadby, Ian T., Moynihan, Patrick J., Lovering, Andrew L.

“…The bacterial second messenger cyclic-di-GMP is a widespread, prominent effector of lifestyle change. An example of this occurs in the predatory bacterium…”
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The hydrolase LpqI primes mycobacterial peptidoglycan recycling by Moynihan, Patrick J., Cadby, Ian T., Veerapen, Natacha, Jankute, Monika, Crosatti, Marialuisa, Mukamolova, Galina V., Lovering, Andrew L., Besra, Gurdyal S.

“…Growth and division by most bacteria requires remodelling and cleavage of their cell wall. A byproduct of this process is the generation of free peptidoglycan…”
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The mycobacterial glycoside hydrolase LamH enables capsular arabinomannan release and stimulates growth by Franklin, Aaron, Salgueiro, Vivian C., Layton, Abigail J., Sullivan, Rudi, Mize, Todd, Vázquez-Iniesta, Lucía, Benedict, Samuel T., Gurcha, Sudagar S., Anso, Itxaso, Besra, Gurdyal S., Banzhaf, Manuel, Lovering, Andrew L., Williams, Spencer J., Guerin, Marcelo E., Scott, Nichollas E., Prados-Rosales, Rafael, Lowe, Elisabeth C., Moynihan, Patrick J.

“…Mycobacterial glycolipids are important cell envelope structures that drive host-pathogen interactions. Arguably, the most important are lipoarabinomannan…”
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CdbA is a DNA-binding protein and c-di-GMP receptor important for nucleoid organization and segregation in Myxococcus xanthus by Skotnicka, Dorota, Steinchen, Wieland, Szadkowski, Dobromir, Cadby, Ian T., Lovering, Andrew L., Bange, Gert, Søgaard-Andersen, Lotte

“…Cyclic di-GMP (c-di-GMP) is a second messenger that modulates multiple responses to environmental and cellular signals in bacteria. Here we identify CdbA, a…”
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Author Correction: The mycobacterial glycoside hydrolase LamH enables capsular arabinomannan release and stimulates growth by Franklin, Aaron, Salgueiro, Vivian C., Layton, Abigail J., Sullivan, Rudi, Mize, Todd, Vázquez-Iniesta, Lucía, Benedict, Samuel T., Gurcha, Sudagar S., Anso, Itxaso, Besra, Gurdyal S., Banzhaf, Manuel, Lovering, Andrew L., Williams, Spencer J., Guerin, Marcelo E., Scott, Nichollas E., Prados-Rosales, Rafael, Lowe, Elisabeth C., Moynihan, Patrick J.

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Antibacterial T6SS effectors with a VRR-Nuc domain are structure-specific nucleases by Hespanhol, Julia Takuno, Sanchez-Limache, Daniel Enrique, Nicastro, Gianlucca Gonçalves, Mead, Liam, Llontop, Edgar Enrique, Chagas-Santos, Gustavo, Farah, Chuck Shaker, de Souza, Robson Francisco, Galhardo, Rodrigo da Silva, Lovering, Andrew L, Bayer-Santos, Ethel

“…The type VI secretion system (T6SS) secretes antibacterial effectors into target competitors. spp. encode five phylogenetically distinct T6SSs. Here, we…”
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Structure-Function Characterization of the Conserved Regulatory Mechanism of the Escherichia coli M48 Metalloprotease BepA by Bryant, Jack A, Cadby, Ian T, Chong, Zhi-Soon, Boelter, Gabriela, Sevastsyanovich, Yanina R, Morris, Faye C, Cunningham, Adam F, Kritikos, George, Meek, Richard W, Banzhaf, Manuel, Chng, Shu-Sin, Lovering, Andrew L, Henderson, Ian R

“…The asymmetric Gram-negative outer membrane (OM) is the first line of defense for bacteria against environmental insults and attack by antimicrobials. The key…”
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Interrupting peptidoglycan deacetylation during Bdellovibrio predator-prey interaction prevents ultimate destruction of prey wall, liberating bacterial-ghosts by Lambert, Carey, Lerner, Thomas R., Bui, Nhat Khai, Somers, Hannah, Aizawa, Shin-Ichi, Liddell, Susan, Clark, Ana, Vollmer, Waldemar, Lovering, Andrew L., Sockett, R. Elizabeth

“…The peptidoglycan wall, located in the periplasm between the inner and outer membranes of the cell envelope in Gram-negative bacteria, maintains cell shape and…”
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Nucleotide signaling pathway convergence in a cAMP‐sensing bacterial c‐di‐GMP phosphodiesterase by Cadby, Ian T, Basford, Sarah M, Nottingham, Ruth, Meek, Richard, Lowry, Rebecca, Lambert, Carey, Tridgett, Matthew, Till, Rob, Ahmad, Rashidah, Fung, Rowena, Hobley, Laura, Hughes, William S, Moynihan, Patrick J, Sockett, R Elizabeth, Lovering, Andrew L

“…Bacterial usage of the cyclic dinucleotide c‐di‐GMP is widespread, governing the transition between motile/sessile and unicellular/multicellular behaviors…”
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Specialized peptidoglycan hydrolases sculpt the intra-bacterial niche of predatory Bdellovibrio and increase population fitness by Lerner, Thomas R, Lovering, Andrew L, Bui, Nhat Khai, Uchida, Kaoru, Aizawa, Shin-ichi, Vollmer, Waldemar, Sockett, R Elizabeth

“…Bdellovibrio are predatory bacteria that have evolved to invade virtually all gram-negative bacteria, including many prominent pathogens. Upon invasion, prey…”
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Ras GTPase-like protein MglA, a controller of bacterial social-motility in Myxobacteria, has evolved to control bacterial predation by Bdellovibrio by Milner, David S, Till, Rob, Cadby, Ian, Lovering, Andrew L, Basford, Sarah M, Saxon, Emma B, Liddell, Susan, Williams, Laura E, Sockett, R Elizabeth

“…Bdellovibrio bacteriovorus invade Gram-negative bacteria in a predatory process requiring Type IV pili (T4P) at a single invasive pole, and also glide on…”
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The lifestyle switch protein Bd0108 of Bdellovibrio bacteriovorus is an intrinsically disordered protein by Prehna, Gerd, Ramirez, Benjamin E, Lovering, Andrew L

“…Bdellovibrio bacteriovorus is a δ-proteobacterium that preys upon Salmonella spp., E. coli, and other Gram-negative bacteria. Bdellovibrio can grow axenically…”
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Activity of Bdellovibrio hit locus proteins, Bd0108 and Bd0109, links Type IVa pilus extrusion/retraction status to prey-independent growth signalling by Capeness, Michael J, Lambert, Carey, Lovering, Andrew L, Till, Rob, Uchida, Kaoru, Chaudhuri, Roy, Alderwick, Luke J, Lee, David J, Swarbreck, David, Liddell, Susan, Aizawa, Shin-Ichi, Sockett, Renee Elizabeth

“…Bdellovibrio bacteriovorus are facultatively predatory bacteria that grow within gram-negative prey, using pili to invade their periplasmic niche. They also…”
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Life in the “Old Bag” Yet: Structure of Peptidoglycan L,D-Carboxypeptidases by Cadby, Ian T., Lovering, Andrew L.

“…In this issue of Structure, Hoyland and colleagues describe the structure of a peptidoglycan L,D-carboxypeptidase in both substrate-bound and apoenzyme forms…”
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Identification of Dynamic Structural Motifs Involved in Peptidoglycan Glycosyltransfer by Lovering, Andrew L., De Castro, Liza, Strynadka, Natalie C.J.

“…We have determined the structure of a new form of the bifunctional peptidoglycan glycosyltransferase (GT)/transpeptidase penicillin-binding protein 2 from the…”
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