scholarly journals Inhibitor Recognition Specificity of MERS-CoV Papain-like Protease May Differ from That of SARS-CoV

2015 ◽  
Vol 10 (6) ◽  
pp. 1456-1465 ◽  
Author(s):  
Hyun Lee ◽  
Hao Lei ◽  
Bernard D. Santarsiero ◽  
Joseph L. Gatuz ◽  
Shuyi Cao ◽  
...  
Keyword(s):  
Recognition Specificity ◽  
Inhibitor Recognition

Sequence and Structural Diversity of the S Locus Genes From Different Lines With the Same Self-Recognition Specificities in Brassica oleracea

Genetics ◽  
2000 ◽  
Vol 154 (1) ◽  
pp. 413-420 ◽  
Author(s):  
Makoto Kusaba ◽  
Masanori Matsushita ◽  
Keiichi Okazaki ◽  
Yoko Satta ◽  
Takeshi Nishio
Keyword(s):  
Structural Diversity ◽  
Receptor Protein ◽  
Self Incompatibility ◽  
S Locus ◽  
High Similarity ◽  
Putative Receptor ◽  
Recognition Specificity ◽  
Polymorphic Genes ◽  
Self Recognition ◽  
Self Fertilization

Abstract Self-incompatibility (SI) is a mechanism for preventing self-fertilization in flowering plants. In Brassica, it is controlled by a single multi-allelic locus, S, and it is believed that two highly polymorphic genes in the S locus, SLG and SRK, play central roles in self-recognition in stigmas. SRK is a putative receptor protein kinase, whose extracellular domain exhibits high similarity to SLG. We analyzed two pairs of lines showing cross-incompatibility (S2 and S2-b; S13 and S13-b). In S2 and S2-b, SRKs were more highly conserved than SLGs. This was also the case with S13 and S13-b. This suggests that the SRKs of different lines must be conserved for the lines to have the same self-recognition specificity. In particular, SLG2-b showed only 88.5% identity to SLG2, which is comparable to that between the SLGs of different S haplotypes, while SRK2-b showed 97.3% identity to SRK2 in the S domain. These findings suggest that the SLGs in these S haplotypes are not important for self-recognition in SI.

scholarly journals The Advances and Challenges of NK Cell-Based Cancer Immunotherapy

2021 ◽  
Vol 28 (2) ◽  
pp. 1077-1093
Author(s):  
Synat Kang ◽  
Xuefeng Gao ◽  
Li Zhang ◽  
Erna Yang ◽  
Yonghui Li ◽  
...  
Keyword(s):  
Nk Cells ◽  
Cancer Immunotherapy ◽  
Nk Cell ◽  
Tumor Development ◽  
Human Leukocyte ◽  
Cell Receptor ◽  
Clinical Applications ◽  
Therapeutic Approaches ◽  
Leukocyte Antigens ◽  
Recognition Specificity

Natural killer (NK) cells can be widely applied for cancer immunotherapy due to their ability to lyse tumor targets without prior sensitization or human leukocyte antigens-matching. Several NK-based therapeutic approaches have been attempted in clinical practice, but their efficacy is not sufficient to suppress tumor development mainly because of lacking specificity. To this end, the engineering of NK cells with T cell receptor along with CD3 subunits (TCR-NK) has been developed to increase the reactivity and recognition specificity of NK cells toward tumor cells. Here, we review recent advances in redirecting NK cells for cancer immunotherapy and discuss the major challenges and future explorations for their clinical applications.

Luteolin Imprinted Polymer with Selective Recognition and Adsorption Performance

2014 ◽  
Vol 809-810 ◽  
pp. 297-301
Author(s):  
Ping Rui Meng ◽  
Liang Bo Li
Keyword(s):  
Adsorption Process ◽  
Selective Adsorption ◽  
Methanol Solution ◽  
Selective Recognition ◽  
Imprinted Polymer ◽  
Molecular Imprinted Polymers ◽  
Adsorption Dynamics ◽  
Adsorption Performance ◽  
Recognition Specificity ◽  
Adsorption Amount

In order to selectively separate luteolin from its crude solution, we synthesized luteolin molecular imprinted polymers (LMIP) with high recognition specificity for luteolin, using an imprinting technique. Luteolin was used as template, methanol as solvent, and N,N’-methylenebisacrylamide (MBAA) as the cross-linking. Then prepared LMIP were characterized and evaluated by scanning electron microscope (SEM) and equilibrium absorption experiments. The results showed that the cavities matching with the template molecules in size and structure were present in the LMIP. Adsorption dynamics analysis suggested that, when the adsorption time reached 4 h, the adsorption process had reached balance and the adsorption capacity was at steady state. The selective adsorption amount reached at 35.65 umol/g for the LMIP, while a lower value of 11.68 umol/g for the blank polymer (i.e. nontemplated). Relative to the corresponding blank polymer, LMIP had an excellent recognition to luteolin in methanol solution. Keywords: Molecular imprinting, Molecular recognition, Adsorbent, Luteolin

scholarly journals Sibling Rivalry in Myxococcus xanthus Is Mediated by Kin Recognition and a Polyploid Prophage

2016 ◽  
Vol 198 (6) ◽  
pp. 994-1004 ◽  
Author(s):  
Arup Dey ◽  
Christopher N. Vassallo ◽  
Austin C. Conklin ◽  
Darshankumar T. Pathak ◽  
Vera Troselj ◽  
...  
Keyword(s):  
Cell Surface ◽  
Kin Recognition ◽  
Myxococcus Xanthus ◽  
Laboratory Strain ◽  
Cell Surface Receptor ◽  
Form Complex ◽  
Content Type ◽  
Recognition Specificity ◽  
Surface Receptor ◽  
Evolutionary Event

ABSTRACTMyxobacteria form complex social communities that elicit multicellular behaviors. One such behavior is kin recognition, in which cells identify siblings via their polymorphic TraA cell surface receptor, to transiently fuse outer membranes and exchange their contents. In addition, outer membrane exchange (OME) regulates behaviors, such as inhibition of wild-typeMyxococcus xanthus(DK1622) from swarming. Here we monitored the fate of motile cells and surprisingly found they were killed by nonmotile siblings. The kill phenotype required OME (i.e., was TraA dependent). The genetic basis of killing was traced to ancestral strains used to construct DK1622. Specifically, the kill phenotype mapped to a large “polyploid prophage,” Mx alpha. Sensitive strains contained a 200-kb deletion that removed two of three Mx alpha units. To explain these results, we suggest that Mx alpha expresses a toxin-antitoxin cassette that uses the OME machinery ofM. xanthusto transfer a toxin that makes the population “addicted” to Mx alpha. Thus, siblings that lost Mx alpha units (no immunity) are killed by cells that harbor the element. To test this, an Mx alpha-harboring laboratory strain was engineered (bytraAallele swap) to recognize a closely related species,Myxococcus fulvus. As a result,M. fulvus, which lacks Mx alpha, was killed. These TraA-mediated antagonisms provide an explanation for how kin recognition specificity might have evolved in myxobacteria. That is, recognition specificity is determined by polymorphisms intraA, which we hypothesize were selected for because OME with non-kin leads to lethal outcomes.IMPORTANCEThe transition from single cell to multicellular life is considered a major evolutionary event. Myxobacteria have successfully made this transition. For example, in response to starvation, individual cells aggregate into multicellular fruiting bodies wherein cells differentiate into spores. To build fruits, cells need to recognize their siblings, and in part, this is mediated by the TraA cell surface receptor. Surprisingly, we report that TraA recognition can also involve sibling killing. We show that killing originates from a prophage-like element that has apparently hijacked the TraA system to deliver a toxin to kin. We hypothesize that this killing system has imposed selective pressures on kin recognition, which in turn has resulted in TraA polymorphisms and hence many different recognition groups.

scholarly journals Ligand Recognition Specificity of Leukocyte Integrin αMβ2 (Mac-1, CD11b/CD18) and Its Functional Consequences

Biochemistry ◽  
2015 ◽  
Vol 54 (6) ◽  
pp. 1408-1420 ◽  
Author(s):  
Nataly P. Podolnikova ◽  
Andriy V. Podolnikov ◽  
Thomas A. Haas ◽  
Valeryi K. Lishko ◽  
Tatiana P. Ugarova
Keyword(s):  
Ligand Recognition ◽  
Recognition Specificity ◽  
Functional Consequences

The unique functional role of the C–H⋯S hydrogen bond in the substrate specificity and enzyme catalysis of type 1 methionine aminopeptidase

2016 ◽  
Vol 12 (8) ◽  
pp. 2408-2416 ◽  
Author(s):  
Ravikumar Reddi ◽  
Kiran Kumar Singarapu ◽  
Debnath Pal ◽  
Anthony Addlagatta
Keyword(s):  
Hydrogen Bonding ◽  
Enzyme Catalysis ◽  
Functional Role ◽  
Methionine Aminopeptidase ◽  
Recognition Specificity ◽  
Hydrogen Bonding Interactions ◽  
Polar Interactions ◽  
Aminopeptidase P

Unique C–H⋯S hydrogen bonding interactions allow nature to attain recognition specificity between molecular interfaces where there is no apparent scope for classical hydrogen bonding or polar interactions.

scholarly journals The allelic rice immune receptor Pikh confers extended resistance to strains of the blast fungus through a single polymorphism in the effector binding interface

2021 ◽  
Vol 17 (3) ◽  
pp. e1009368
Author(s):  
Juan Carlos De la Concepcion ◽  
Josephine H. R. Maidment ◽  
Apinya Longya ◽  
Gui Xiao ◽  
Marina Franceschetti ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Allelic Variation ◽  
Immune Recognition ◽  
In Planta ◽  
Pathogen Effectors ◽  
Binding Interface ◽  
Recognition Specificity ◽  
Blast Fungus ◽  
Resistance Specificity ◽  
Mechanistic Basis

Arms race co-evolution drives rapid adaptive changes in pathogens and in the immune systems of their hosts. Plant intracellular NLR immune receptors detect effectors delivered by pathogens to promote susceptibility, activating an immune response that halts colonization. As a consequence, pathogen effectors evolve to escape immune recognition and are highly variable. In turn, NLR receptors are one of the most diverse protein families in plants, and this variability underpins differential recognition of effector variants. The molecular mechanisms underlying natural variation in effector recognition by NLRs are starting to be elucidated. The rice NLR pair Pik-1/Pik-2 recognizes AVR-Pik effectors from the blast fungus Magnaporthe oryzae, triggering immune responses that limit rice blast infection. Allelic variation in a heavy metal associated (HMA) domain integrated in the receptor Pik-1 confers differential binding to AVR-Pik variants, determining resistance specificity. Previous mechanistic studies uncovered how a Pik allele, Pikm, has extended recognition to effector variants through a specialized HMA/AVR-Pik binding interface. Here, we reveal the mechanistic basis of extended recognition specificity conferred by another Pik allele, Pikh. A single residue in Pikh-HMA increases binding to AVR-Pik variants, leading to an extended effector response in planta. The crystal structure of Pikh-HMA in complex with an AVR-Pik variant confirmed that Pikh and Pikm use a similar molecular mechanism to extend their pathogen recognition profile. This study shows how different NLR receptor alleles functionally converge to extend recognition specificity to pathogen effectors.

scholarly journals Recognition Specificity for the Bacterial Avirulence Protein AvrPto Is Determined by Thr-204 in the Activation Loop of the Tomato Pto Kinase

1998 ◽  
Vol 2 (2) ◽  
pp. 241-245 ◽  
Author(s):  
Reid D. Frederick ◽  
Roger L. Thilmony ◽  
Guido Sessa ◽  
Gregory B. Martin
Keyword(s):  
Activation Loop ◽  
Recognition Specificity ◽  
Pto Kinase

scholarly journals Characterization of a novel anti-peptide antibody that recognizes a specific conformation of the platelet-derived growth factor receptor.

1988 ◽  
Vol 8 (9) ◽  
pp. 3696-3702 ◽  
Author(s):  
S Bishayee ◽  
S Majumdar ◽  
C D Scher ◽  
S Khan
Keyword(s):  
Growth Factor ◽  
Growth Factor Receptor ◽  
Platelet Derived Growth Factor ◽  
Pdgf Receptor ◽  
Amino Acid Residues ◽  
Site Specific ◽  
Recognition Specificity ◽  
Peptide Antibody ◽  
Peptide Antibodies

Two site-specific anti-peptide antibodies (AbP1 and AbP2) were raised against the platelet-derived growth factor (PDGF) receptor. These two sites correspond to amino acid residues 977 through 988 (peptide 1) and 932 through 947 (peptide 2) of the murine PDGF receptor. Both antibodies recognized human and murine PDGF receptors in immunoprecipitation and immunoblotting analyses. None of the antibodies was directed to phosphotyrosine. One of the antibodies (AbP2) showed unusual antigen recognition specificity. This antibody specifically recognized the tyrosine-phosphorylated PDGF receptor and not the unphosphorylated native receptor, suggesting that recognition by this antibody requires a specific conformation that is induced by PDGF-stimulated autophosphorylation.

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