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Chapter 17 : Innate Immunity against Bacteria

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Innate Immunity against Bacteria, Page 1 of 2

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Abstract:

The innate immune response to bacteria has been a major determinant of natural selection and evolution throughout the plant and animal kingdoms. The association between host and microbe can be symbiotic or can give rise to devastating epidemics of infectious disease. The innate mechanisms of resistance to bacteria and other organisms remain a priority for investigation, as does their connection to adaptive immunity, vaccine development, and autoimmunity. LPS stimulation of macrophages induced RIG-I expression and RIG-I- deficient macrophages exhibited impaired phagocytosis, while RIG-I-deficient mice were more susceptible to infection. The granules of neutrophils contain several different serine proteases, including elastase, cathepsin G, and protease 3 that effectively kill engulfed bacteria. The generation of mice deficient in elastase or cathepsin G has demonstrated that these molecules are crucial for resistance against infection with selected gram-positive or gram-negative pathogens. Many milestones were achieved in the 20th century, such as delineation of leukocyte differentiation and activation; the description of surface receptors for opsonic and nonopsonic recognition of microbes, especially the Toll like receptors (TLR) and signaling pathways; molecular characterization of cytokines such as TNF and interferon-γ (IFN-γ) and other mediators of cellular interaction, bacterial killing, and inflammation. This chapter summarizes cellular and humoral mechanisms of innate immunity to bacteria in mammals. The authors consider microbial ligands that serve as recognition structures for cellular receptors, secreted bactericidal molecules, and humoral proteins, such as complement components and pentraxins.

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17

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Figures

Image of FIGURE 1a
FIGURE 1a

Innate immune receptors. Schematic structures of selected surface glycoproteins expressed by myeloid leukocytes. (A) Recognition receptors, to illustrate the variety of nonopsonic receptors (CD11b/CD18 is also an opsonic receptor for complement). N and C indicate orientation. (B) Regulatory molecules and paired receptors. See text and references for details ( ).

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17
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Image of FIGURE 1b
FIGURE 1b

Innate immune receptors. Schematic structures of selected surface glycoproteins expressed by myeloid leukocytes. (A) Recognition receptors, to illustrate the variety of nonopsonic receptors (CD11b/CD18 is also an opsonic receptor for complement). N and C indicate orientation. (B) Regulatory molecules and paired receptors. See text and references for details ( ).

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17
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Image of FIGURE 2
FIGURE 2

Selected bacterial pathogens evade distinct phagocytic mechanisms. Pathogenic bacteria have developed several mechanisms to enter and survive inside macrophages. Following an LPS-dependent, lipid raft-mediated entry, is found in an early containing vacuole (BCV) that acquires early endosome markers Rab5 and EEA-1. BCVs then mature into acidic intermediate vacuoles that accumulate LAMP-1, but not Rab7, avoiding interactions with late endosomes and fusion with lysosomes. BCVs then interact with ER exit sites (via VirB type IV secretion system) leading to fusion with the ER, generating an ER-derived organelle permissive for bacterial replication. Replicative BCVs exclude LAMP-1 and acquire various ER markers as a result of membrane exchange with the ER. Bacterial replication is thought to occur through fission of the BCV into two daughter BCVs via further accretion of ER membranes. resides and multiplies in a vacuole studded with ribosomes due to interaction with the rough endoplasmic reticulum (RER). The organism inhibits acidification of its phagosome and secretes effector molecules via its type IV secretion system into the cell, which inhibit phagosome/lysosome fusion. The phagosome acquires the early endosome markers EEA1 and Rab5 and then matures into a late endosome defined by the presence of the markers Lamp1, Lamp2, and Rab7. The late endosome does not acidify and the phagosomal membrane is disrupted, releasing the bacteria into the cytosol. The phagosome acquires the early endosome marker Rab5 but excludes the late endosomal Lamps and Rab7. Mycobacteria have characteristic thick cell wall, which is hydrophobic, waxy, and rich in mycolic acids/mycolates and allows them to survive inside phagosomes. This organism also inhibits acidification of the phagosome and produces molecules that block fusion with the lysosome, allowing it to reside and replicate in this modified phagosome. Acidification of the phagosome is essential for the perforation of the phagosomal membrane and escape of the bacteria into the cytosol. Here they mobilize the cell’s own actin polymerization machinery (via the bacterial ActA protein) to move within the cell and then from cell to cell ( ).

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17
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FIGURE 3

Macrophage sensing of intracellular serovar Typhimurium is mediated by detection of monomeric flagellin, which is secreted by the bacterial type III secretion system and is dependent on the S. Typhimurium SipB protein. Upon stimulation, inactive monomeric Nlrc4 (formerly IPAF, ICE-protease activating factor) oligomerizes to form active NLRC4 inflammasome. The NLRC4 inflammasome then recruits ASC (apoptosis-associated speck-like protein containing a CARD system), which, in turn, recruits procaspase-1. Proteolytic cleavage activates caspase-1, which induces release of interleukin-1β, interleukin-18, and macrophage cell death. NLRC4 is also involved in sensing of and Sensing of is mediated by the bacterial type III secretion system protein lpaB. sensing is mediated by Naip5 (neuronal apoptosis inhibitor protein 5) detection of monomeric flagellin secreted by the type IV secretion system, which induces caspase-1 in conjunction with NLRC4. and produce microbial toxins (e.g., maitotoxin, aerolysin, nigericin) and activate other signals (ATP and uric acid), which activate the NLPR3 inflammasome. This results in activation of caspase-1, and active caspase-1 can then process pro-IL-1β and pro-IL-18 and induce macrophage cell death. The specific NOD-like receptor (NLR) protein that detects intracellular remains to be identified; however, ASC is essential in the immune response against CARD, caspase-recruitment domain; LRR, leucine-rich repeat; NACHT, domain present in NAIP, CIITA, HET E and TP1. (For further details see ).

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17
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Tables

Generic image for table
TABLE 1

Selected properties of innate leukocytes, with reference to bacterial infection

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17
Generic image for table
TABLE 2

Selected bacterial ligands recognized by the innate immune system

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17
Generic image for table
TABLE 3

Properties of selected innate recognition membrane receptors

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17
Generic image for table
TABLE 4

Properties of selected membrane molecules that regulate myeloid cell innate responses

Citation: Areschoug T, Plüddemann A, Gordon S. 2011. Innate Immunity against Bacteria, p 209-223. In Kaufmann S, Rouse B, Sacks D (ed), The Immune Response to Infection. ASM Press, Washington, DC. doi: 10.1128/9781555816872.ch17

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