Journal articles: 'ANTIMICROBIAL DEFENSE'

1

Cove, Jonathan H., and E. Anne Eady. "Cutaneous antimicrobial defense." Clinics in Dermatology 16, no. 1 (January 1998): 141–47. http://dx.doi.org/10.1016/s0738-081x(97)00177-6.

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2

Visan, Ioana. "Nociceptors in antimicrobial defense." Nature Immunology 21, no. 2 (January 24, 2020): 103. http://dx.doi.org/10.1038/s41590-019-0586-8.

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3

Meister, Marie, Bruno Lemaitre, and Jules A. Hoffmann. "Antimicrobial peptide defense inDrosophila." BioEssays 19, no. 11 (November 1997): 1019–26. http://dx.doi.org/10.1002/bies.950191112.

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4

Castro, Mariana, and Wagner Fontes. "Plant Defense and Antimicrobial Peptides." Protein & Peptide Letters 12, no. 1 (January 1, 2005): 11–16. http://dx.doi.org/10.2174/0929866053405832.

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5

Brubaker, S. W., and D. M. Monack. "Microbial metabolite triggers antimicrobial defense." Science 348, no. 6240 (June 11, 2015): 1207–8. http://dx.doi.org/10.1126/science.aac5835.

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6

Brown, Kelly L., and Robert EW Hancock. "Cationic host defense (antimicrobial) peptides." Current Opinion in Immunology 18, no. 1 (February 2006): 24–30. http://dx.doi.org/10.1016/j.coi.2005.11.004.

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7

Mukherjee, Sohini, and Lora V. Hooper. "Antimicrobial Defense of the Intestine." Immunity 42, no. 1 (January 2015): 28–39. http://dx.doi.org/10.1016/j.immuni.2014.12.028.

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8

Sahl, Hans Georg. "Optimizing Antimicrobial Host Defense Peptides." Chemistry & Biology 13, no. 10 (October 2006): 1015–17. http://dx.doi.org/10.1016/j.chembiol.2006.10.001.

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Kwiecien, Kamila, Aneta Zegar, James Jung, Piotr Brzoza, Mateusz Kwitniewski, Urszula Godlewska, Beata Grygier, Patrycja Kwiecinska, Agnieszka Morytko, and Joanna Cichy. "Architecture of antimicrobial skin defense." Cytokine & Growth Factor Reviews 49 (October 2019): 70–84. http://dx.doi.org/10.1016/j.cytogfr.2019.08.001.

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10

Simanski, Maren, Bente Köten, Jens-Michael Schröder, Regine Gläser, and Jürgen Harder. "Antimicrobial RNases in Cutaneous Defense." Journal of Innate Immunity 4, no. 3 (2012): 241–47. http://dx.doi.org/10.1159/000335029.

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Bilej, M., P. De Baetselier, and A. Beschin. "Antimicrobial defense of the earthworm." Folia Microbiologica 45, no. 4 (August 2000): 283–300. http://dx.doi.org/10.1007/bf02817549.

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12

Munro, Nancy. "Antimicrobial Resistance." AACN Advanced Critical Care 26, no. 3 (July 1, 2015): 225–30. http://dx.doi.org/10.4037/nci.0000000000000102.

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The health care system is challenged by another serious issue: antimicrobial resistance. Clostridium difficile is the most common infection in health care institutions and is becoming resistant to standard treatment. Carbapenem-resistant enterobacteriaceae can be found in almost every state in the United States. Confounding the antimicrobial resistance issue is the fact that few new antimicrobials are being developed by pharmaceutical companies. The situation is so critical that the White House issued a strategic plan in September 2014 to deal with antimicrobial resistance. One challenge in that plan is to better understand how microbes have become resistant. Microbes have developed defense mechanisms such as bacteriophages and bacteriocins to survive for thousands of years. If science can start to use these mechanisms to help combat resistant organisms in combination with antimicrobials and strong epidemiological interventions, the battle against antimicrobial resistance may succeed.

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13

Jenssen, Håvard, Pamela Hamill, and Robert E. W. Hancock. "Peptide Antimicrobial Agents." Clinical Microbiology Reviews 19, no. 3 (July 2006): 491–511. http://dx.doi.org/10.1128/cmr.00056-05.

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SUMMARY Antimicrobial host defense peptides are produced by all complex organisms as well as some microbes and have diverse and complex antimicrobial activities. Collectively these peptides demonstrate a broad range of antiviral and antibacterial activities and modes of action, and it is important to distinguish between direct microbicidal and indirect activities against such pathogens. The structural requirements of peptides for antiviral and antibacterial activities are evaluated in light of the diverse set of primary and secondary structures described for host defense peptides. Peptides with antifungal and antiparasitic activities are discussed in less detail, although the broad-spectrum activities of such peptides indicate that they are important host defense molecules. Knowledge regarding the relationship between peptide structure and function as well as their mechanism of action is being applied in the design of antimicrobial peptide variants as potential novel therapeutic agents.

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Cytryńska, Małgorzata, and Agnieszka Zdybicka-Barabas. "Defense peptides: recent developments." Biomolecular Concepts 6, no. 4 (August 1, 2015): 237–51. http://dx.doi.org/10.1515/bmc-2015-0014.

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AbstractDefense peptides are small amphipathic molecules that exhibit antimicrobial, antitumor, antiviral, and immunomodulatory properties. This review summarizes current knowledge on the mechanisms of antimicrobial activity of cationic and anionic defense peptides, indicating peptide-based as well as microbial cell-based factors affecting this activity. The peptide-based factors include charge, hydrophibicity, and amphipathicity, whereas the pathogen-based factors are membrane lipid composition, presence of sterols, membrane fluidity, cell wall components, and secreted factors such as extracellular proteinases. Since defense peptides have been considered very promising molecules that could replace conventional antibiotics in the era of drug-resistant pathogens, the issue of microbial resistance to antimicrobial peptides (AMPs) is addressed. Furthermore, selected approaches employed for optimization and de novo design of effective AMPs based on the properties recognized as important for the function of natural defense peptides are presented.

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15

Patocka, Jiri, Eugenie Nepovimova, Blanka Klimova, Qinghua Wu, and Kamil Kuca. "Antimicrobial Peptides: Amphibian Host Defense Peptides." Current Medicinal Chemistry 26, no. 32 (November 19, 2019): 5924–46. http://dx.doi.org/10.2174/0929867325666180713125314.

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Antimicrobial Peptides (AMPs) are one of the most common components of the innate immune system that protect multicellular organisms against microbial invasion. The vast majority of AMPs are isolated from the frog skin. Anuran (frogs and toads) skin contains abundant AMPs that can be developed therapeutically. Such peptides are a unique but diverse group of molecules. In general, more than 50% of the amino acid residues form the hydrophobic part of the molecule. Normally, there are no conserved structural motifs responsible for activity, although the vast majority of the AMPs are cationic due to the presence of multiple lysine residues; this cationicity has a close relationship with antibacterial activity. Notably, recent evidence suggests that synthesis of AMPs in frog skin may confer an advantage on a particular species, although they are not essential for survival. Frog skin AMPs exert potent activity against antibiotic-resistant bacteria, protozoa, yeasts, and fungi by permeating and destroying the plasma membrane and inactivating intracellular targets. Importantly, since they do not bind to a specific receptor, AMPs are less likely to induce resistance mechanisms. Currently, the best known amphibian AMPs are esculentins, brevinins, ranacyclins, ranatuerins, nigrocin-2, magainins, dermaseptins, bombinins, temporins, and japonicins-1 and -2, and palustrin-2. This review focuses on these frog skin AMPs and the mechanisms underlying their antimicrobial activity. We hope that this review will provide further information that will facilitate further study of AMPs and cast new light on novel and safer microbicides.

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Fritig, Bernard, Thierry Heitz, and Michel Legrand. "Antimicrobial proteins in induced plant defense." Current Opinion in Immunology 10, no. 1 (February 1998): 16–22. http://dx.doi.org/10.1016/s0952-7915(98)80025-3.

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17

Kraus, Dirk, and Andreas Peschel. "Staphylococcus aureusevasion of innate antimicrobial defense." Future Microbiology 3, no. 4 (August 2008): 437–51. http://dx.doi.org/10.2217/17460913.3.4.437.

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18

Braff, Marissa H., Antoanella Bardan, Victor Nizet, and Richard L. Gallo. "Cutaneous Defense Mechanisms by Antimicrobial Peptides." Journal of Investigative Dermatology 125, no. 1 (July 2005): 9–13. http://dx.doi.org/10.1111/j.0022-202x.2004.23587.x.

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19

Li, Chun, Hans-Matti Blencke, Tor Haug, and Klara Stensvåg. "Antimicrobial peptides in echinoderm host defense." Developmental & Comparative Immunology 49, no. 1 (March 2015): 190–97. http://dx.doi.org/10.1016/j.dci.2014.11.002.

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20

Arnason, John T., and Mark A. Bernards. "Impact of constitutive plant natural products on herbivores and pathogensThe present review is one in the special series of reviews on animal–plant interactions." Canadian Journal of Zoology 88, no. 7 (July 2010): 615–27. http://dx.doi.org/10.1139/z10-038.

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Plants defend themselves from pests with deterrent or toxic phytochemicals. In addition to the development of preformed mechanical barriers such as cutin and suberin, the first line of defense for plants against pathogens and herbivores is constitutive (preformed) biologically active inhibitors. Because of the adaptation of insects and pathogens to these inhibitors, plants have evolved a stunning diversity of new and different bioactive molecules to combat pests. Some representative mechanisms of plant defense include the use of antimicrobial, anitfeedant, and phototoxic molecules. Examples of natural product defenses of specific plant families are also described. Diversity and redundancy in plant defenses is key to slowing pest resistance to host-plant defenses.

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21

Wertz, Philip W., and Sarah de Szalay. "Innate Antimicrobial Defense of Skin and Oral Mucosa." Antibiotics 9, no. 4 (April 3, 2020): 159. http://dx.doi.org/10.3390/antibiotics9040159.

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This special issue intends to review and update our understanding of the antimicrobial defense mechanisms of the skin and oral cavity. These two environments are quite different in terms of water, pH, and nutrient availability, but have some common antimicrobial factors. The skin surface supports the growth of a limited range of microorganisms but provides a hostile environment for others. The growth of most microorganisms is prevented or limited by the low pH, scarcity of some nutrients such as phosphorus and the presence of antimicrobial peptides, including defensins and cathelicidins, and antimicrobial lipids, including certain fatty acids and long-chain bases. On the other hand, the oral cavity is a warm, moist, nutrient rich environment which supports the growth of diverse microflora. Saliva coating the oral soft and hard surfaces determines which microorganisms can adhere to these surfaces. Some salivary proteins bind to bacteria and prevent their attachment to surfaces. Other salivary peptides, including defensins, cathelicidins, and histatins are antimicrobial. Antimicrobial salivary proteins include lysozyme, lactoferrin, and lactoperoxidase. There are also antimicrobial fatty acids derived from salivary triglycerides and long-chain bases derived from oral epithelial sphingolipids. The various antimicrobial factors determine the microbiomes of the skin surface and the oral cavity. Alterations of these factors can result in colonization by opportunistic pathogens, and this may lead to infection. Neutrophils and lymphocytes in the connective tissue of skin and mucosa also contribute to innate immunity.

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22

Lyu, Wentao, Amanda Curtis, Lakshmi Sunkara, and Guolong Zhang. "Transcriptional Regulation of Antimicrobial Host Defense Peptides." Current Protein & Peptide Science 16, no. 7 (August 10, 2015): 672–79. http://dx.doi.org/10.2174/1389203716666150630133432.

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23

Yan, Hong, and Robert E. W. Hancock. "Synergistic Interactions between Mammalian Antimicrobial Defense Peptides." Antimicrobial Agents and Chemotherapy 45, no. 5 (May 1, 2001): 1558–60. http://dx.doi.org/10.1128/aac.45.5.1558-1560.2001.

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ABSTRACT A single animal can express several cationic antimicrobial peptides with different sequences and structures. We demonstrate that mammalian peptides from different structural classes frequently show synergy with each other and selectively show synergy with human lysozyme.

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24

Mohammed, Imran, Dalia G. Said, and Harminder S. Dua. "Human antimicrobial peptides in ocular surface defense." Progress in Retinal and Eye Research 61 (November 2017): 1–22. http://dx.doi.org/10.1016/j.preteyeres.2017.03.004.

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25

Mukherjee, S., S. Vaishnava, and L. V. Hooper. "Multi-layered regulation of intestinal antimicrobial defense." Cellular and Molecular Life Sciences 65, no. 19 (June 17, 2008): 3019–27. http://dx.doi.org/10.1007/s00018-008-8182-3.

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26

Landman, Sanne L., Maaike E. Ressing, and Annemarthe G. van der Veen. "Balancing STING in antimicrobial defense and autoinflammation." Cytokine & Growth Factor Reviews 55 (October 2020): 1–14. http://dx.doi.org/10.1016/j.cytogfr.2020.06.004.

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27

Ganz, Tomas. "Antimicrobial peptides: from host defense to therapeutics." AIDS 15 (February 2001): S57. http://dx.doi.org/10.1097/00002030-200102001-00080.

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28

Haine, E. R., Y. Moret, M. T. Siva-Jothy, and J. Rolff. "Antimicrobial Defense and Persistent Infection in Insects." Science 322, no. 5905 (November 21, 2008): 1257–59. http://dx.doi.org/10.1126/science.1165265.

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29

Mitta, Guillaume, Franck Vandenbulcke, Florence Hubert, Michel Salzet, and Philippe Roch. "Involvement of Mytilins in Mussel Antimicrobial Defense." Journal of Biological Chemistry 275, no. 17 (April 21, 2000): 12954–62. http://dx.doi.org/10.1074/jbc.275.17.12954.

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30

D’Alba, Liliana, and Matthew D. Shawkey. "Mechanisms of antimicrobial defense in avian eggs." Journal of Ornithology 156, S1 (May 1, 2015): 399–408. http://dx.doi.org/10.1007/s10336-015-1226-1.

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31

Chen, Xian-Ming, Silu Deng, Ai-Yu Gong, Yang Wang, Xin-Tian Zhang, Min Li, Juan Li, and Nicholas W. Mathy. "Induction of a long non-coding RNA, lncRNA-Chr1:1226, by Cryptosporidium infection primes intestinal epithelial cells for IFN-γ-mediated host antimicrobial gene transcription." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 190.12. http://dx.doi.org/10.4049/jimmunol.202.supp.190.12.

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Abstract Cryptosporidium, a protozoan parasite that infects the intestinal epithelium and other mucosal surfaces in animals and humans, is an important opportunistic pathogen in AIDS patients and a common cause of diarrhea in young children in developing countries. Intestinal epithelial cellular defense is key to innate mucosal anti-Cryptosporidium defense but underlying molecular mechanisms are still obscure. Here, we identified several long non-coding RNAs (lncRNAs) that are predominantly expressed in intestinal epithelial cells. Several of such epithelial-enriched lncRNAs, such as lncRNA-Chr1:1226, were upregulated in cells following C. parvum infection. Induction of lncRNA-Chr1:1226 in infected intestinal epithelial cells was controlled by TLR4/NF-κB/Cdc42 signaling and epithelial specific transcription factor Eif3. Induction of lncRNA-Chr1:1226 promoted IFN-γ-mediated epithelial antimicrobial defense, through facilitating STAT1/SWI/SNF-associated chromatin remodeling to promote IFN-γ-mediated transcription of defense genes in intestinal epithelial cells. We observed that IFN-γ-mediated antimicrobial defense was suppressed in neonatal intestinal epithelium. Expression of PRDM1 in the neonatal intestinal epithelium might contribute to suppression of IFN-γ-mediated antimicrobial gene transcription. Furthermore, PRDM1 interacted with lncRNA-Chr1:1226 and PIAS1 to attenuate SWI/SNF-mediated antimicrobial transcription induced by IFN-γ in intestinal epithelium of neonates. Our data demonstrate that lncRNAs, particularly epithelial lncRNAs, may be key regulators in IFN-γ-mediated epithelial defense.

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32

Patel, Seema, and Nadeem Akhtar. "Antimicrobial peptides (AMPs): The quintessential ‘offense and defense’ molecules are more than antimicrobials." Biomedicine & Pharmacotherapy 95 (November 2017): 1276–83. http://dx.doi.org/10.1016/j.biopha.2017.09.042.

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33

Lee, Ernest Y., Liana C. Chan, Huiyuan Wang, Juelline Lieng, Mandy Hung, Yashes Srinivasan, Jennifer Wang, et al. "PACAP is a pathogen-inducible resident antimicrobial neuropeptide affording rapid and contextual molecular host defense of the brain." Proceedings of the National Academy of Sciences 118, no. 1 (December 28, 2020): e1917623117. http://dx.doi.org/10.1073/pnas.1917623117.

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Defense of the central nervous system (CNS) against infection must be accomplished without generation of potentially injurious immune cell-mediated or off-target inflammation which could impair key functions. As the CNS is an immune-privileged compartment, inducible innate defense mechanisms endogenous to the CNS likely play an essential role in this regard. Pituitary adenylate cyclase-activating polypeptide (PACAP) is a neuropeptide known to regulate neurodevelopment, emotion, and certain stress responses. While PACAP is known to interact with the immune system, its significance in direct defense of brain or other tissues is not established. Here, we show that our machine-learning classifier can screen for immune activity in neuropeptides, and correctly identified PACAP as an antimicrobial neuropeptide in agreement with previous experimental work. Furthermore, synchrotron X-ray scattering, antimicrobial assays, and mechanistic fingerprinting provided precise insights into how PACAP exerts antimicrobial activities vs. pathogens via multiple and synergistic mechanisms, including dysregulation of membrane integrity and energetics and activation of cell death pathways. Importantly, resident PACAP is selectively induced up to 50-fold in the brain in mouse models of Staphylococcus aureus or Candida albicans infection in vivo, without inducing immune cell infiltration. We show differential PACAP induction even in various tissues outside the CNS, and how these observed patterns of induction are consistent with the antimicrobial efficacy of PACAP measured in conditions simulating specific physiologic contexts of those tissues. Phylogenetic analysis of PACAP revealed close conservation of predicted antimicrobial properties spanning primitive invertebrates to modern mammals. Together, these findings substantiate our hypothesis that PACAP is an ancient neuro-endocrine-immune effector that defends the CNS against infection while minimizing potentially injurious neuroinflammation.

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34

Leonor Sánchez, Mercedes, Melina María Belén Martínez, and Paulo César Maffia. "Natural Antimicrobial Peptides: Pleiotropic Molecules in Host Defense." CellBio 02, no. 04 (2013): 200–210. http://dx.doi.org/10.4236/cellbio.2013.24023.

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35

Drayton, Matthew, Julia P. Deisinger, Kevin C. Ludwig, Nigare Raheem, Anna Müller, Tanja Schneider, and Suzana K. Straus. "Host Defense Peptides: Dual Antimicrobial and Immunomodulatory Action." International Journal of Molecular Sciences 22, no. 20 (October 16, 2021): 11172. http://dx.doi.org/10.3390/ijms222011172.

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The rapid rise of multidrug-resistant (MDR) bacteria has once again caused bacterial infections to become a global health concern. Antimicrobial peptides (AMPs), also known as host defense peptides (HDPs), offer a viable solution to these pathogens due to their diverse mechanisms of actions, which include direct killing as well as immunomodulatory properties (e.g., anti-inflammatory activity). HDPs may hence provide a more robust treatment of bacterial infections. In this review, the advent of and the mechanisms that lead to antibiotic resistance will be described. HDP mechanisms of antibacterial and immunomodulatory action will be presented, with specific examples of how the HDP aurein 2.2 and a few of its derivatives, namely peptide 73 and cG4L73, function. Finally, resistance that may arise from a broader use of HDPs in a clinical setting and methods to improve biocompatibility will be briefly discussed.

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36

Libardo, M. Daben J., and Alfredo M. Angeles-Boza. "Bioinorganic Chemistry of Antimicrobial and Host-Defense Peptides." Comments on Inorganic Chemistry 34, no. 1-2 (January 2, 2014): 42–58. http://dx.doi.org/10.1080/02603594.2014.960923.

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37

Nicolas, Pierre. "Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides." FEBS Journal 276, no. 22 (October 10, 2009): 6483–96. http://dx.doi.org/10.1111/j.1742-4658.2009.07359.x.

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38

North, Robert J., Pamela L. Dunn, and J. Wayne Conlan. "Murine listeriosis as a model of antimicrobial defense." Immunological Reviews 158, no. 1 (August 1997): 27–36. http://dx.doi.org/10.1111/j.1600-065x.1997.tb00989.x.

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39

Yeaman, Michael R. "The Role of Platelets in Antimicrobial Host Defense." Clinical Infectious Diseases 25, no. 5 (November 1997): 951–68. http://dx.doi.org/10.1086/516120.

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40

Hosaka, Yoshio, Maureen Koslowski, Sabine Nuding, Guoxing Wang, Miriam Schlee, Christian Schäfer, Katunori Saigenji, Eduard F. Stange, and Jan Wehkamp. "Antimicrobial host defense in the upper gastrointestinal tract." European Journal of Gastroenterology & Hepatology 20, no. 12 (December 2008): 1151–58. http://dx.doi.org/10.1097/meg.0b013e3283052ddb.

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41

Huttner, Kenneth M., and Charles L. Bevins. "Antimicrobial Peptides as Mediators of Epithelial Host Defense." Pediatric Research 45, no. 6 (June 1999): 785–94. http://dx.doi.org/10.1203/00006450-199906000-00001.

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42

Chung, Lawton K., and Manuela Raffatellu. "G.I. pros: Antimicrobial defense in the gastrointestinal tract." Seminars in Cell & Developmental Biology 88 (April 2019): 129–37. http://dx.doi.org/10.1016/j.semcdb.2018.02.001.

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43

Schroder, Kate, and Vojo Deretic. "Innate immunity, the constant gardener of antimicrobial defense." Current Opinion in Microbiology 16, no. 3 (June 2013): 293–95. http://dx.doi.org/10.1016/j.mib.2013.06.007.

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44

Steinstraesser, Lars, Ursula Kraneburg, Frank Jacobsen, and Sammy Al-Benna. "Host defense peptides and their antimicrobial-immunomodulatory duality." Immunobiology 216, no. 3 (March 2011): 322–33. http://dx.doi.org/10.1016/j.imbio.2010.07.003.

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45

Mehrad, Borna, and Theodore J. Standiford. "Role of cytokines in pulmonary antimicrobial host defense." Immunologic Research 20, no. 1 (August 1999): 15–27. http://dx.doi.org/10.1007/bf02786504.

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46

Schauber, Jürgen, and Richard L. Gallo. "Antimicrobial peptides and the skin immune defense system." Journal of Allergy and Clinical Immunology 122, no. 2 (August 2008): 261–66. http://dx.doi.org/10.1016/j.jaci.2008.03.027.

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47

Schauber, Jürgen, and Richard L. Gallo. "Antimicrobial peptides and the skin immune defense system." Journal of Allergy and Clinical Immunology 124, no. 3 (September 2009): R13—R18. http://dx.doi.org/10.1016/j.jaci.2009.07.014.

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48

Büchau, Amanda S., and Richard L. Gallo. "Innate immunity and antimicrobial defense systems in psoriasis." Clinics in Dermatology 25, no. 6 (November 2007): 616–24. http://dx.doi.org/10.1016/j.clindermatol.2007.08.016.

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49

Ma, Yanan, King Lam Hui, Zaza Gelashvili, and Philipp Niethammer. "Oxoeicosanoid signaling mediates early antimicrobial defense in zebrafish." Cell Reports 42, no. 1 (January 2023): 111974. http://dx.doi.org/10.1016/j.celrep.2022.111974.

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50

Gross, Jürgen, Kerstin Schumacher, Henrike Schmidtberg, and Andreas Vilcinskas. "Protected by Fumigants: Beetle Perfumes in Antimicrobial Defense." Journal of Chemical Ecology 34, no. 2 (January 31, 2008): 179–88. http://dx.doi.org/10.1007/s10886-007-9416-9.

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Journal articles on the topic 'ANTIMICROBIAL DEFENSE'

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