Lysozymes in the Animal Kingdom

Tullio, Vivian; Spaccapelo, Roberta; Polimeni, Manuela

doi:10.1007/978-3-319-09432-8_3

Cited by 8 publications

(16 citation statements)

References 94 publications

(106 reference statements)

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“…It is a relatively small biomolecule at 14,307 Da in mass, comprising of two domains and a cleft in the protein centre which acts as the active site 16 . The secondary structure of each domain differs significantly, with one domain mainly β-sheet in structure and the other mainly helical 17 . Its main role is to attack the cell walls of bacteria, breaking the cell wall and causing the bacteria to burst under their own internal pressure.…”

Section: Introductionmentioning

confidence: 99%

“…Its main role is to attack the cell walls of bacteria, breaking the cell wall and causing the bacteria to burst under their own internal pressure. 17 Lysozyme AuNCs (Ly-AuNCs) have been shown to make excellent probes for the detection of mercury 15 and glutathione 18 , in vitro experiments; to date no experiments using Ly-AuNCs in vivo as fluorescent probes have been carried out. The functionality of Lysozyme after AuNC synthesis has been shown to still be present to some degree as Liu et.…”

Section: Introductionmentioning

confidence: 99%

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Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

Russell

Jachimska

Komorek

et al. 2017

Phys. Chem. Chem. Phys.

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The study of gold nanoclusters (AuNCs) has seen much interest in recent history due to their unique fluorescence properties and environmentally friendly synthesis method using proteins as a growth scaffold. The differences in the physicochemical properties of lysozyme encapsulated AuNCs in comparison to natural lysozyme are characterised in order to determine the effects AuNCs have on natural protein behaviour. The hydrodynamic radius (dynamic light scattering), light absorbance (UV-Vis), electrophoretic mobility, relative density, dynamic viscosity, adsorption (quartz crystal microbalance) and circular dichroism (CD) characteristics of the molecules were studied. It was found that lysozyme forms small dimer/trimer aggregates upon the synthesis of AuNCs within the protein. The diameter of Ly-AuNCs was found to be 8.0 nm across a pH range of 2-11 indicating dimer formation, but larger aggregates with diameters >20 nm were formed between pH 3 and 6. The formation of larger aggregates limits the use of Ly-AuNCs as a fluorescent probe in this pH range. A large shift in the protein's isoelectric point was also observed, shifting from 11.0 to 4.0 upon AuNC synthesis. This resulted in major changes to the adsorption characteristics of lysozyme, observed using a QCM. A monolayer of 8 nm was seen for Ly-AuNCs at pH 4, offering further evidence that the proteins form small aggregates, unlike the natural monomer form of lysozyme. The adsorption of Ly-AuNCs was seen to decrease as pH was increased; this is in major contrast to the lysozyme adsorption behaviour. A decrease in the α-helix content was observed from 25% in natural lysozyme to 1% in Ly-AuNCs. This coincided with an increase in the β-sheet content after AuNC synthesis indicating that the natural structure of lysozyme was lost. The formation of protein dimers, the change in the protein surface charge from positive to negative, and secondary structure alteration caused by the AuNC synthesis must be considered before attempting to utilise Ly-AuNCs as in vivo probes.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

Russell

Jachimska

Komorek

et al. 2017

Phys. Chem. Chem. Phys.

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“…Lysozymes are enzymes that hydrolyse the b-(1,4)-linked N-acetylglucosamine (NAG) and N-acteylmuramic (NAM) acid residues in the peptidoglycan of bacterial cells and are important components of the innate immune system (Callewaert et al, 2008(Callewaert et al, , 2012Callewaert & Michiels, 2010). Peptidoglycan is an essential and unique cross-linked cell wall heteropolymer in bacteria (Callewaert et al, 2012).…”

Section: Lysozyme Resistance In Pathogenic Bacteriamentioning

confidence: 99%

“…Peptidoglycan is an essential and unique cross-linked cell wall heteropolymer in bacteria (Callewaert et al, 2012). The peptidoglycan forms a sacculus around the entire cell and its main function is to provide protection against turgor pressure (Callewaert et al, 2008(Callewaert et al, , 2012Callewaert & Michiels, 2010). In a hypo-osmotic environment, loss of peptidoglycan integrity results in rapid cells lysis (Callewaert & Michiels, 2010).…”

Section: Lysozyme Resistance In Pathogenic Bacteriamentioning

confidence: 99%

“…The peptidoglycan forms a sacculus around the entire cell and its main function is to provide protection against turgor pressure (Callewaert et al, 2008(Callewaert et al, , 2012Callewaert & Michiels, 2010). In a hypo-osmotic environment, loss of peptidoglycan integrity results in rapid cells lysis (Callewaert & Michiels, 2010). Lysozyme has the capacity to kill pathogenic bacteria, and the peptidoglycan fragments released by lysozyme are recognized by a variety of immune receptors triggering, an immune response (Park & Uehara, 2008;Reith & Mayer, 2011).…”

Section: Lysozyme Resistance In Pathogenic Bacteriamentioning

confidence: 99%

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The role of the anti-σ factor RsiV in stress response in Clostridium difficile and Bacillus subtilis

Castro¹

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I have learned so much throughout my graduate career. Thank you to my fellow graduate students, lab mates, family and friends. First, thank you to my advisor Craig Ellermeier. You have provided me with support, advice, encouragement to become an independent scientist and gave me the freedom to pursue interesting projects. Also, thank you for not getting mad every time I decorated your office with Iowa Hawkeye décor. To my thesis committee, Tim and David, thank you for your continued encouragement and contribution. To the Ellermeier lab, thank you for your unwavering support. I looked forward to going to lab every day and you made it easy for me to learn and grow. T, thank you for always being available to chat and grab sweet potato fries. Lincoln, Ute, Kelsie and Gabriela, thank you for the conversations that ranged from science, cycling, climbing and sports. To the crystallography core, thank you Sankar and Lokesh for teaching me about protein work and allowing me to ask many questions. To the graduate students, thank you for making my transition into the Microbiology program an easy one. To Kayley, thank you for always having a listening ear and for helping me train for my first 5K. Thank you to everyone in the Microbiology office for your willingness to help. Finally, I would like to thank my family. To my parents Delia and Benigno, my sister Digna, brothers Eduardo and Nino, my many nieces and nephews, and to my fiancé for always encouraging me, even when they had no idea what I was working on.

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Chemically Modified Bacterial Sacculi as a Vaccine Microparticle Scaffold

et al. 2022

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Vaccine scaffolds and carrier proteins increase the immunogenicity of subunit vaccines. Here, we developed, characterized, and demonstrated the efficacy of a novel microparticle vaccine scaffold comprised of bacterial peptidoglycan (PGN), isolated as an entire sacculi. The PGN microparticles contain bio-orthogonal chemical handles allowing for site-specific attachment of immunogens. We first evaluated the purification, integrity, and immunogenicity of PGN microparticles derived from a variety of bacterial species. We then optimized PGN microparticle modification conditions; Staphylococcus aureus PGN microparticles containing azido- d -alanine yielded robust conjugation to immunogens. We then demonstrated that this vaccine scaffold elicits comparable immunostimulation to the conventional carrier protein, keyhole limpet hemocyanin (KLH). We further modified the S. aureus PGN microparticle to contain the SARS-CoV-2 receptor-binding domain (RBD)—this conjugate vaccine elicited neutralizing antibody titers comparable to those elicited by the KLH-conjugated RBD. Collectively, these findings suggest that chemically modified bacterial PGN microparticles are a conjugatable and biodegradable microparticle scaffold capable of eliciting a robust immune response toward an antigen of interest.

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Lysozymes in the Animal Kingdom

Cited by 8 publications

References 94 publications

Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

The role of the anti-σ factor RsiV in stress response in Clostridium difficile and Bacillus subtilis

Chemically Modified Bacterial Sacculi as a Vaccine Microparticle Scaffold

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