scholarly journals Functional and Structural Diversity in the Als Protein Family ofCandida albicans

2004 ◽  
Vol 279 (29) ◽  
pp. 30480-30489 ◽  
Author(s):  
Donald C. Sheppard ◽  
Michael R. Yeaman ◽  
William H. Welch ◽  
Quynh T. Phan ◽  
Yue Fu ◽  
...  
Keyword(s):  
Structural Diversity ◽  
Protein Family ◽  
Ofcandida Albicans

scholarly journals Profiling of adhesive properties of the agglutinin-like sequence (ALS) protein family, a virulent attribute ofCandida albicans

2012 ◽  
Vol 65 (1) ◽  
pp. 121-124 ◽  
Author(s):  
Wataru Aoki ◽  
Nao Kitahara ◽  
Natsuko Miura ◽  
Hironobu Morisaka ◽  
Kouichi Kuroda ◽  
...  
Keyword(s):  
Protein Family ◽  
Adhesive Properties ◽  
Ofcandida Albicans

Plant Thaumatin-like Proteins: Function, Evolution and Biotechnological Applications

2020 ◽  
Vol 21 (1) ◽  
pp. 36-51 ◽  
Author(s):  
Carolline de Jesús-Pires ◽  
José Ribamar Costa Ferreira-Neto ◽  
João Pacifico Bezerra-Neto ◽  
Ederson Akio Kido ◽  
Roberta Lane de Oliveira Silva ◽  
...  
Keyword(s):  
Fungal Pathogens ◽  
Structural Diversity ◽  
Protein Family ◽  
Structure Evolution ◽  
Biotic And Abiotic Stresses ◽  
Biotechnological Potential ◽  
Biotic Stresses ◽  
Therapeutic Drugs ◽  
Pathogenesis Related ◽  
Complex Protein

Thaumatin-like proteins (TLPs) are a highly complex protein family associated with host defense and developmental processes in plants, animals, and fungi. They are highly diverse in angiosperms, for which they are classified as the PR-5 (Pathogenesis-Related-5) protein family. In plants, TLPs have a variety of properties associated with their structural diversity. They are mostly associated with responses to biotic stresses, in addition to some predicted activities under drought and osmotic stresses. The present review covers aspects related to the structure, evolution, gene expression, and biotechnological potential of TLPs. The efficiency of the discovery of new TLPs is below its potential, considering the availability of omics data. Furthermore, we present an exemplary bioinformatics annotation procedure that was applied to cowpea (Vigna unguiculata) transcriptome, including libraries of two tissues (root and leaf), and two stress types (biotic/abiotic) generated using different sequencing approaches. Even without using genomic sequences, the pipeline uncovered 56 TLP candidates in both tissues and stresses. Interestingly, abiotic stress (root dehydration) was associated with a high number of modulated TLP isoforms. The nomenclature used so far for TLPs was also evaluated, considering TLP structure and possible functions identified to date. It is clear that plant TLPs are promising candidates for breeding purposes and for plant transformation aiming a better performance under biotic and abiotic stresses. The development of new therapeutic drugs against human fungal pathogens also deserves attention. Despite that, applications derived from TLP molecules are still below their potential, as it is evident in our review.

scholarly journals An Allergen Portrait Gallery: Representative Structures and an Overview of IgE Binding Surfaces

2010 ◽  
Vol 4 ◽  
pp. BBI.S5737 ◽  
Author(s):  
Catherine H. Schein ◽  
Ovidiu Ivanciuc ◽  
Terumi Midoro-Horiuti ◽  
Randall M. Goldblum ◽  
Werner Braun
Keyword(s):  
Recent Progress ◽  
Structural Diversity ◽  
Protein Family ◽  
Structural Determination ◽  
Computational Results ◽  
Ige Binding ◽  
Molecular Determinants ◽  
Allergenic Proteins ◽  
Protein Classes

Recent progress in the biochemical classification and structural determination of allergens and allergen–antibody complexes has enhanced our understanding of the molecular determinants of allergenicity. Databases of allergens and their epitopes have facilitated the clustering of allergens according to their sequences and, more recently, their structures. Groups of similar sequences are identified for allergenic proteins from diverse sources, and all allergens are classified into a limited number of protein structural families. A gallery of experimental structures selected from the protein classes with the largest number of allergens demonstrate the structural diversity of the allergen universe. Further comparison of these structures and identification of areas that are different from innocuous proteins within the same protein family can be used to identify features specific to known allergens. Experimental and computational results related to the determination of IgE binding surfaces and methods to define allergen-specific motifs are highlighted.

scholarly journals Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum

Parasitology ◽  
2012 ◽  
Vol 139 (10) ◽  
pp. 1231-1245 ◽  
Author(s):  
IAIN W. CHALMERS ◽  
KARL F. HOFFMANN
Keyword(s):  
Immune Response ◽  
Functional Characterization ◽  
Structural Diversity ◽  
Host Immune Response ◽  
Comprehensive Analysis ◽  
Protein Family ◽  
Host Interactions ◽  
Venom Allergen

SUMMARYDuring platyhelminth infection, a cocktail of proteins is released by the parasite to aid invasion, initiate feeding, facilitate adaptation and mediate modulation of the host immune response. Included amongst these proteins is the Venom Allergen-Like (VAL) family, part of the larger sperm coating protein/Tpx-1/Ag5/PR-1/Sc7 (SCP/TAPS) superfamily. To explore the significance of this protein family during Platyhelminthes development and host interactions, we systematically summarize all published proteomic, genomic and immunological investigations of the VAL protein family to date. By conducting new genomic and transcriptomic interrogations to identify over 200 VAL proteins (228) from species in all 4 traditional taxonomic classes (Trematoda, Cestoda, Monogenea and Turbellaria), we further expand our knowledge related to platyhelminth VAL diversity across the phylum. Subsequent phylogenetic and tertiary structural analyses reveal several class-specific VAL features, which likely indicate a range of roles mediated by this protein family. Our comprehensive analysis of platyhelminth VALs represents a unifying synopsis for understanding diversity within this protein family and a firm context in which to initiate future functional characterization of these enigmatic members.

Investigating the functional link between TMEM165 and SPCA1

2019 ◽  
Vol 476 (21) ◽  
pp. 3281-3293 ◽  
Author(s):  
Elodie Lebredonchel ◽  
Marine Houdou ◽  
Hans-Heinrich Hoffmann ◽  
Kateryna Kondratska ◽  
Marie-Ange Krzewinski ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Complete Loss ◽  
Protein Family ◽  
Uncharacterized Protein ◽  
Functional Link ◽  
P Type

TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper, we establish a functional link between TMEM165 and SPCA1, the Golgi Ca2+/Mn2+ P-type ATPase pump. A nearly complete loss of TMEM165 was observed in SPCA1-deficient Hap1 cells. We demonstrate that TMEM165 was constitutively degraded in lysosomes in the absence of SPCA1. Complementation studies showed that TMEM165 abundance was directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. Among SPCA1 mutants that differentially impair Mn2+ and Ca2+ transport, only the Q747A mutant that favors Mn2+ pumping rescues the abundance and Golgi subcellular localization of TMEM165. Interestingly, the overexpression of SERCA2b also rescues the expression of TMEM165. Finally, this paper highlights that TMEM165 expression is linked to the function of SPCA1.

The involvement of the GGA protein family in BACE transport and APP processing in Alzheimer's disease

2008 ◽  
Vol 35 (S 01) ◽  
Author(s):  
C Steinmetz ◽  
B von Einem ◽  
D Schwanzar ◽  
F Dolp ◽  
A.C Ludolph ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Family ◽  
App Processing

Metal-, and Organocatalyst-Free One-Pot Assembly of Chiral Aza-Tricyclic Molecules: Creating Six Contiguous Stereocenters from 2-D-Structures and an Amino Acid

2020 ◽  
Author(s):  
Dung Do
Keyword(s):  
Amino Acid ◽  
Chemical Space ◽  
Structural Diversity ◽  
Therapeutic Agents ◽  
Chiral Molecules ◽  
One Pot ◽  
Complex Molecules ◽  
Chiral Catalyst ◽  
Chiral Complex ◽  
Free Process

<p>Chiral molecules with their defined 3-D structures are of paramount importance for the study of chemical biology and drug discovery. Having rich structural diversity and unique stereoisomerism, chiral molecules offer a large chemical space that can be explored for the design of new therapeutic agents.<sup>1</sup> Practically, chiral architectures are usually prepared from organometallic and organocatalytic processes where a transition metal or an organocatalyst is tailor-made for desired reactions. As a result, developing a method that enables rapid assembly of chiral complex molecules under metal- and organocatalyst-free condition represents a daunting challenge. Here we developed a straightforward route to create a chiral 3-D structure from 2-D structures and an amino acid without any chiral catalyst. The center of this research is the design of a <a>special chiral spiroimidazolidinone cyclohexadienone intermediate</a>, a merger of a chiral reactive substrate with multiple nucleophillic/electrophillic sites and a transient organocatalyst. <a>This unique substrate-catalyst (“subcatalyst”) dual role of the intermediate enhances </a><a>the coordinational proximity of the chiral substrate and catalyst</a> in the key Aza-Michael/Michael cascade resulting in a substantial steric discrimination and an excellent overall diastereoselectivity. Whereas the “subcatalyst” (hidden catalyst) is not present in the reaction’s initial components, which renders a chiral catalyst-free process, it is strategically produced to promote sequential self-catalyzed reactions. The success of this methodology will pave the way for many efficient preparations of chiral complex molecules and aid for the quest to create next generation of therapeutic agents.</p>

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