Self/nonselfPub Date : 2010-04-01Epub Date: 2010-03-06DOI: 10.4161/self.1.2.11717
Roberto Biassoni, Elisabetta Ugolotti, Andrea De Maria
{"title":"Comparative analysis of NK-cell receptor expression and function across primate species: Perspective on antiviral defenses.","authors":"Roberto Biassoni, Elisabetta Ugolotti, Andrea De Maria","doi":"10.4161/self.1.2.11717","DOIUrl":"https://doi.org/10.4161/self.1.2.11717","url":null,"abstract":"Natural killer (NK) cells are lymphoid effectors that are involved in the innate immune surveillance against infected and/or tumor cells. Their function is under the fine-tuning control of cell surface receptors that display either inhibitory or activating function and in healthy condition, mediate self-tolerance. It is known that inhibitory receptors are characterized by clonal and stochastic distribution and are extremely sensible to any modification, downregulation or loss of MHC class I surface expression that are induced in autologous cells upon viral infection or cancer transformation. This alteration of the MHC class I expression weakens the strength of the inhibitory receptor-induced interaction, thus resulting in a prompt triggering of NK cell function, which ends up in the inhibition of tumor progression and proliferation of pathogen-infected cells. Thus, the inhibitory function of NK cells is only one face of the coin, since NK-cell activation is controlled by different arrays of activating receptors that finally are involved in the induction of cytolysis and/or cytokine release. Interestingly, the inhibitory NK-cell receptors that are involved in dampening NK cell-mediated responses evolved during speciation in different, often structurally unrelated surface-expressed molecules, all using a conserved signaling pathway. In detail, during evolution, the inhibitory receptors that assure the recognition of MHC class I molecules, originate in, at least, three different ways. This ended up in multigene families showing marked structural divergences that coevolved in a convergent way with the availability of appropriate MHC ligand molecules.","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 2","pages":"103-113"},"PeriodicalIF":0.0,"publicationDate":"2010-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/self.1.2.11717","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29698790","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Self/nonselfPub Date : 2010-04-01Epub Date: 2010-02-15DOI: 10.4161/self.1.2.11550
Mark D Mannie
{"title":"Autoimmunity and asthma: The dirt on the hygiene hypothesis.","authors":"Mark D Mannie","doi":"10.4161/self.1.2.11550","DOIUrl":"https://doi.org/10.4161/self.1.2.11550","url":null,"abstract":"<p><p>Self peptides shape T-cell development through selectional processes in the thymus and secondary lymphoid organs to promote a diverse and balanced repertoire of conventional and regulatory T cells. Foreign proteins and their derivative peptides permeate our mucosal tissues to constitute another diverse array of peptides that may specify and diversify the mucosal T-cell repertoire. Indeed, the distinction between self peptides and environmental foreign peptides may be academic if both are present constantly within the body. The premise here is that the plethora of foreign peptides, present ubiquitously in our environment and body, form homeostatic niches to foster highly diversified repertoires of conventional and regulatory T cells that recognize persistent environmental peptides as self. Highly diversified repertoires that recognize myriads of self and environmental foreign peptides as homeostatic ligands may be critical for adaptive distinctions of friend or foe in mucosal tissues. The change from our agrarian past to the highly sterile environments of today may adversely impact the diversity and concentrations of foreign peptides that shape the mucosal T-cell repertoire. Various hygiene hypotheses postulate that the lack of factors such as infectious pathogens, innate receptor engagement or Th1 bias is key to the marked increase in immunological disease in modern society. In this version of the hygiene hypothesis, highly diverse constellations of innocuous environmental peptides are postulated to be the critical factor for immune balance and homeostasis.</p>","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 2","pages":"123-128"},"PeriodicalIF":0.0,"publicationDate":"2010-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/self.1.2.11550","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29749426","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Self/nonselfPub Date : 2010-04-01Epub Date: 2010-02-17DOI: 10.4161/self.1.2.11547
Alexander B Sigalov
{"title":"Membrane binding of intrinsically disordered proteins: Critical importance of an appropriate membrane model.","authors":"Alexander B Sigalov","doi":"10.4161/self.1.2.11547","DOIUrl":"https://doi.org/10.4161/self.1.2.11547","url":null,"abstract":"","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 2","pages":"129-132"},"PeriodicalIF":0.0,"publicationDate":"2010-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/self.1.2.11547","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29749427","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Self/nonselfPub Date : 2010-01-01DOI: 10.4161/self.1.1.9588
Brett Trost, Anthony Kusalik, Guglielmo Lucchese, Darja Kanduc
{"title":"Bacterial peptides are intensively present throughout the human proteome.","authors":"Brett Trost, Anthony Kusalik, Guglielmo Lucchese, Darja Kanduc","doi":"10.4161/self.1.1.9588","DOIUrl":"https://doi.org/10.4161/self.1.1.9588","url":null,"abstract":"<p><p>Forty bacterial proteomes-20 pathogens and 20 non-pathogens-were examined for amino acid sequence similarity to the human proteome. All bacterial proteomes, independent of their pathogenicity, share hundreds of nonamer sequences with the human proteome. This overlap is very widespread, with one third of human proteins sharing at least one nonapeptide with one of these bacteria. On the whole, the bacteria-versus-human nonamer overlap is numerically defined by 47,610 total perfect matches disseminated through 10,701 human proteins. These findings open new perspectives on the immune relationship between bacteria and host, and might help our understanding of fundamental phenomena such as self-nonself discrimination and tolerance versus auto-reactivity.</p>","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 1","pages":"71-74"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/self.1.1.9588","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30174718","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Self/nonselfPub Date : 2010-01-01DOI: 10.4161/self.1.1.10441
Yan-Ming Liu, Jing Luo, Clive Bennett
{"title":"Adaptive immunity: Based on the dual recognition responses of αβT cells.","authors":"Yan-Ming Liu, Jing Luo, Clive Bennett","doi":"10.4161/self.1.1.10441","DOIUrl":"https://doi.org/10.4161/self.1.1.10441","url":null,"abstract":"<p><p>It is proposed that the recently reported second recognition mode of αβT cells allows an explanation of the evolutionary origin of adaptive immunity. The dual modes provide the mechanism of development/differentiation of αβT cells under the control of immune response (Ir) genes by which a given T-cell can distinguish one kind of MHC molecule (as 'self' phase, learned from its positive selection) from others (as 'nonself' phase) involved in antigen recognition. It is thus possible to re-explain the 'self'/'nonself' concept based on 'homotype (phase)'/'heterotype (phase)' recognition at the level of a single clone of T cells. Hence adaptive immunity is explained here as being derived from functions that ensure synchronous ontogeny and prevent the paradoxical (or retrograde) development of vertebrates.</p>","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 1","pages":"62-66"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/self.1.1.10441","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29872366","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Self/nonselfPub Date : 2010-01-01DOI: 10.4161/self.1.1.10832
Alexander B Sigalov
{"title":"The SCHOOL of nature: I. Transmembrane signaling.","authors":"Alexander B Sigalov","doi":"10.4161/self.1.1.10832","DOIUrl":"10.4161/self.1.1.10832","url":null,"abstract":"<p><p>Receptor-mediated transmembrane signaling plays an important role in health and disease. Recent significant advances in our understanding of the molecular mechanisms linking ligand binding to receptor activation revealed previously unrecognized striking similarities in the basic structural principles of function of numerous cell surface receptors. In this work, I demonstrate that the Signaling Chain Homooligomerization (SCHOOL)-based mechanism represents a general biological mechanism of transmembrane signal transduction mediated by a variety of functionally unrelated single- and multichain activating receptors. within the SCHOOL platform, ligand binding-induced receptor clustering is translated across the membrane into protein oligomerization in cytoplasmic milieu. This platform resolves a long-standing puzzle in transmembrane signal transduction and reveals the major driving forces coupling recognition and activation functions at the level of protein-protein interactions-biochemical processes that can be influenced and controlled. The basic principles of transmembrane signaling learned from the SCHOOL model can be used in different fields of immunology, virology, molecular and cell biology and others to describe, explain and predict various phenomena and processes mediated by a variety of functionally diverse and unrelated receptors. Beyond providing novel perspectives for fundamental research, the platform opens new avenues for drug discovery and development.</p>","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 1","pages":"4-39"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3091606/pdf/self0101_0004.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30174719","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Self/nonselfPub Date : 2010-01-01DOI: 10.4161/self.1.1.10682
William E Paul
{"title":"Self/Nonself-Immune Recognition and Signaling: A new journal tackles a problem at the center of immunological science.","authors":"William E Paul","doi":"10.4161/self.1.1.10682","DOIUrl":"10.4161/self.1.1.10682","url":null,"abstract":"","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 1","pages":"2-3"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3091601/pdf/self0101_0002.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29872364","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Self/nonselfPub Date : 2010-01-01DOI: 10.4161/self.1.1.10442
Natasha M Sanabria, Ju-Chi Huang, Ian A Dubery
{"title":"Self/nonself perception in plants in innate immunity and defense.","authors":"Natasha M Sanabria, Ju-Chi Huang, Ian A Dubery","doi":"10.4161/self.1.1.10442","DOIUrl":"https://doi.org/10.4161/self.1.1.10442","url":null,"abstract":"<p><p>The ability to distinguish 'self' from 'nonself' is the most fundamental aspect of any immune system. The evolutionary solution in plants to the problems of perceiving and responding to pathogens involves surveillance of nonself, damaged-self and altered-self as danger signals. This is reflected in basal resistance or non-host resistance, which is the innate immune response that protects plants against the majority of pathogens. In the case of surveillance of nonself, plants utilize receptor-like proteins or -kinases (RLP/Ks) as pattern recognition receptors (PRRs), which can detect conserved pathogen/microbe-associated molecular pattern (P/MAMP) molecules. P/MAMP detection serves as an early warning system for the presence of a wide range of potential pathogens and the timely activation of plant defense mechanisms. However, adapted microbes express a suite of effector proteins that often interfere or act as suppressors of these defenses. In response, plants have evolved a second line of defense that includes intracellular nucleotide binding leucine-rich repeat (NB-LRR)-containing resistance proteins, which recognize isolate-specific pathogen effectors once the cell wall has been compromised. This host-immunity acts within the species level and is controlled by polymorphic host genes, where resistance protein-mediated activation of defense is based on an 'altered-self' recognition mechanism.</p>","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 1","pages":"40-54"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/self.1.1.10442","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29872367","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Self/nonselfPub Date : 2010-01-01DOI: 10.4161/self.1.1.10663
Martin Poenie
{"title":"Hiways and byways to the secretory synapse.","authors":"Martin Poenie","doi":"10.4161/self.1.1.10663","DOIUrl":"https://doi.org/10.4161/self.1.1.10663","url":null,"abstract":"","PeriodicalId":89270,"journal":{"name":"Self/nonself","volume":"1 1","pages":"69-70"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/self.1.1.10663","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29872368","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}