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Article ; Online: Comparisons of Metabolic Measures to Predict T1D vs. Detect a Preventive Treatment Effect in High-Risk Individuals.

Sims, Emily K / Cuthbertson, David / Jacobsen, Laura / Ismail, Heba M / Nathan, Brandon M / Herold, Kevan C / Redondo, Maria J / Sosenko, Jay

The Journal of clinical endocrinology and metabolism

2024

Abstract: Context: Metabolic measures are frequently used to predict T1D and to understand effects of disease-modifying therapies.: Objective: Compare metabolic endpoints for their ability to detect preventive treatment effects and predict T1D.: Design: Six- ...

Abstract	Context: Metabolic measures are frequently used to predict T1D and to understand effects of disease-modifying therapies. Objective: Compare metabolic endpoints for their ability to detect preventive treatment effects and predict T1D. Design: Six-month changes in metabolic endpoints were assessed for: 1) detecting treatment effects by comparing placebo and treatment arms from the randomized controlled teplizumab prevention trial and 2) predicting T1D in the TrialNet Pathway to Prevention natural history study. Setting: Multicenter clinical trial network. Intervention: 14-day intravenous teplizumab infusion. Main outcome measures: T-values from t tests for detecting a treatment effect were compared to Chi-square values from proportional hazards regression for predicting T1D for each metabolic measure. Patients or other participants: Participants in the teplizumab prevention trial and participants in the Pathway to Prevention study selected with the same inclusion criteria used for the teplizumab trial were studied. Results: Six-month changes in glucose-based endpoints predicted diabetes better than C-peptide-based endpoints, yet the latter were better at detecting a teplizumab effect. Combined measures of glucose and C-peptide were more balanced than measures of glucose alone or C-peptide alone for predicting diabetes and detecting a teplizumab effect. Conclusions: The capacity of a metabolic endpoint to detect a treatment effect does not necessarily correspond to its accuracy for predicting T1D. However, combined glucose and C-peptide endpoints appear to be effective for both predicting diabetes and detecting a response to immunotherapy. These findings suggest that combined glucose and C-peptide endpoints should be incorporated into the design of future T1D prevention trials.
Language	English
Publishing date	2024-01-24
Publishing country	United States
Document type	Journal Article
ZDB-ID	3029-6
ISSN	1945-7197 ; 0021-972X
ISSN (online)	1945-7197
ISSN	0021-972X
DOI	10.1210/clinem/dgae048
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Article ; Online: Phenotypes Associated With Zones Defined by Area Under the Curve Glucose and C-peptide in a Population With Islet Autoantibodies.

Sosenko, Jay M / Cuthbertson, David / Sims, Emily K / Ismail, Heba M / Nathan, Brandon M / Jacobsen, Laura M / Atkinson, Mark A / Evans-Molina, Carmella / Herold, Kevan C / Skyler, Jay S / Redondo, Maria J

Diabetes care

2023 Volume 46, Issue 5, Page(s) 1098–1105

Abstract: Objective: Metabolic zones were developed to characterize heterogeneity of individuals with islet autoantibodies.: Research design and methods: Baseline 2-h oral glucose tolerance test data from 6,620 TrialNet Pathway to Prevention Study (TNPTP) ... ...

Abstract	Objective: Metabolic zones were developed to characterize heterogeneity of individuals with islet autoantibodies. Research design and methods: Baseline 2-h oral glucose tolerance test data from 6,620 TrialNet Pathway to Prevention Study (TNPTP) autoantibody-positive participants (relatives of individuals with type 1 diabetes) were used to form 25 zones from five area under the curve glucose (AUCGLU) rows and five area under the curve C-peptide (AUCPEP) columns. Zone phenotypes were developed from demographic, metabolic, autoantibody, HLA, and risk data. Results: As AUCGLU increased, changes of glucose and C-peptide response curves (from mean glucose and mean C-peptide values at 30, 60, 90, and 120 min) were similar within the five AUCPEP columns. Among the zones, 5-year risk for type 1 diabetes was highly correlated with islet antigen 2 antibody prevalence (r = 0.96, P < 0.001). Disease risk decreased markedly in the highest AUCGLU row as AUCPEP increased (0.88-0.41; P < 0.001 from lowest AUCPEP column to highest AUCPEP column). AUCGLU correlated appreciably less with Index60 (an indicator of insulin secretion) in the highest AUCPEP column (r = 0.33) than in other columns (r ≥ 0.78). AUCGLU was positively related to "fasting glucose × fasting insulin" and to "fasting glucose × fasting C-peptide" (indicators of insulin resistance) before and after adjustments for Index60 (P < 0.001). Conclusions: Phenotypes of 25 zones formed from AUCGLU and AUCPEP were used to gain insights into type 1 diabetes heterogeneity. Zones were used to examine GCRC changes with increasing AUCGLU, associations between risk and autoantibody prevalence, the dependence of glucose as a predictor of risk according to C-peptide, and glucose heterogeneity from contributions of insulin secretion and insulin resistance.
MeSH term(s)	Humans ; Glucose ; Diabetes Mellitus, Type 1 ; Blood Glucose/metabolism ; C-Peptide/metabolism ; Insulin Resistance ; Autoantibodies ; Insulin/metabolism ; Phenotype
Chemical Substances	Glucose (IY9XDZ35W2) ; Blood Glucose ; C-Peptide ; Autoantibodies ; Insulin
Language	English
Publishing date	2023-03-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	441231-x
ISSN	1935-5548 ; 0149-5992
ISSN (online)	1935-5548
ISSN	0149-5992
DOI	10.2337/dc22-2236
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Article ; Online: The Transition From a Compensatory Increase to a Decrease in C-peptide During the Progression to Type 1 Diabetes and Its Relation to Risk.

Ismail, Heba M / Cuthbertson, David / Gitelman, Stephen E / Skyler, Jay S / Steck, Andrea K / Rodriguez, Henry / Atkinson, Mark / Nathan, Brandon M / Redondo, Maria J / Herold, Kevan C / Evans-Molina, Carmella / DiMeglio, Linda A / Sosenko, Jay

Diabetes care

2022 Volume 45, Issue 10, Page(s) 2264–2270

Abstract: Objective: To define the relationship between glucose and C-peptide during the progression to type 1 diabetes (T1D).: Research design and methods: We longitudinally studied glucose and C-peptide response curves (GCRCs), area under curve (AUC) for ... ...

Abstract	Objective: To define the relationship between glucose and C-peptide during the progression to type 1 diabetes (T1D). Research design and methods: We longitudinally studied glucose and C-peptide response curves (GCRCs), area under curve (AUC) for glucose, and AUC C-peptide from oral glucose tolerance tests (OGTTs), and Index60 (which integrates OGTT glucose and C-peptide values) in Diabetes Prevention Trial-Type 1 (DPT-1) (n = 72) and TrialNet Pathway to Prevention Study (TNPTP) (n = 82) participants who had OGTTs at baseline and follow-up time points before diagnosis. Results: Similar evolutions of GCRC configurations were evident between DPT-1 and TNPTP from baseline to 0.5 years prediagnosis. Whereas AUC glucose increased throughout from baseline to 0.5 years prediagnosis, AUC C-peptide increased from baseline until 1.5 years prediagnosis (DPT-1, P = 0.004; TNPTP, P = 0.012) and then decreased from 1.5 to 0.5 years prediagnosis (DPT-1, P = 0.017; TNPTP, P = 0.093). This change was mostly attributable to change in the late AUC C-peptide response (i.e., 60- to 120-min AUC C-peptide). Median Index60 values of DPT-1 (1.44) and TNPTP (1.05) progressors to T1D 1.5 years prediagnosis (time of transition from increasing to decreasing AUC C-peptide) were used as thresholds to identify individuals at high risk for T1D in the full cohort at baseline (5-year risk of 0.75-0.88 for those above thresholds). Conclusions: A transition from an increase to a decrease in AUC C-peptide ∼1.5 years prediagnosis was validated in two independent cohorts. The median Index60 value at that time point can be used as a pathophysiologic-based threshold for identifying individuals at high risk for T1D.
MeSH term(s)	Blood Glucose/metabolism ; C-Peptide/metabolism ; Diabetes Mellitus, Type 1/diagnosis ; Glucose ; Glucose Tolerance Test ; Humans
Chemical Substances	Blood Glucose ; C-Peptide ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2022-08-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	441231-x
ISSN	1935-5548 ; 0149-5992
ISSN (online)	1935-5548
ISSN	0149-5992
DOI	10.2337/dc22-0167
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Article ; Online: Persistence of β-Cell Responsiveness for Over Two Years in Autoantibody-Positive Children With Marked Metabolic Impairment at Screening.

Sims, Emily K / Cuthbertson, David / Felton, Jamie L / Ismail, Heba M / Nathan, Brandon M / Jacobsen, Laura M / Paprocki, Emily / Pugliese, Alberto / Palmer, Jerry / Atkinson, Mark / Evans-Molina, Carmella / Skyler, Jay S / Redondo, Maria J / Herold, Kevan C / Sosenko, Jay M

Diabetes care

2022 Volume 45, Issue 12, Page(s) 2982–2990

Abstract: Objective: We studied longitudinal differences between progressors and nonprogressors to type 1 diabetes with similar and substantial baseline risk.: Research design and methods: Changes in 2-h oral glucose tolerance test indices were used to examine ...

Abstract	Objective: We studied longitudinal differences between progressors and nonprogressors to type 1 diabetes with similar and substantial baseline risk. Research design and methods: Changes in 2-h oral glucose tolerance test indices were used to examine variability in diabetes progression in the Diabetes Prevention Trial-Type 1 (DPT-1) study (n = 246) and Type 1 Diabetes TrialNet Pathway to Prevention study (TNPTP) (n = 503) among autoantibody (Ab)+ children (aged <18.0 years) with similar baseline metabolic impairment (DPT-1 Risk Score [DPTRS] of 6.5-7.5), as well as in TNPTP Ab- children (n = 94). Results: Longitudinal analyses revealed annualized area under the curve (AUC) of C-peptide increases in nonprogressors versus decreases in progressors (P ≤ 0.026 for DPT-1 and TNPTP). Vector indices for AUC glucose and AUC C-peptide changes (on a two-dimensional grid) also differed significantly (P < 0.001). Despite marked baseline metabolic impairment of nonprogressors, changes in AUC C-peptide, AUC glucose, AUC C-peptide-to-AUC glucose ratio (AUC ratio), and Index60 did not differ from Ab- relatives during follow-up. Divergence between nonprogressors and progressors occurred by 6 months from baseline in both cohorts (AUC glucose, P ≤ 0.007; AUC ratio, P ≤ 0.034; Index60, P < 0.001; vector indices of change, P < 0.001). Differences in 6-month change were positively associated with greater diabetes risk (respectively, P < 0.001, P ≤ 0.019, P < 0.001, and P < 0.001) in DPT-1 and TNPTP, except AUC ratio, which was inversely associated with risk (P < 0.001). Conclusions: Novel findings show that even with similarly abnormal baseline risk, progressors had appreciably more metabolic impairment than nonprogressors within 6 months and that the measures showing impairment were predictive of type 1 diabetes. Longitudinal metabolic patterns did not differ between nonprogressors and Ab- relatives, suggesting persistent β-cell responsiveness in nonprogressors.
MeSH term(s)	Child ; Humans ; C-Peptide/metabolism ; Diabetes Mellitus, Type 1/diagnosis ; Blood Glucose/metabolism ; Glucose Tolerance Test ; Autoantibodies ; Glucose ; Disease Progression
Chemical Substances	C-Peptide ; Blood Glucose ; Autoantibodies ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2022-01-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	441231-x
ISSN	1935-5548 ; 0149-5992
ISSN (online)	1935-5548
ISSN	0149-5992
DOI	10.2337/dc22-1362
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Article ; Online: Chapter 4. Evaluating the control of mRNA decay in fission yeast.

Cuthbertson, Brandon J / Blackshear, Perry J

Methods in enzymology

2009 Volume 449, Page(s) 73–95

Abstract: Abnormalities in rates of mRNA decay can lead to changes in steady-state levels of transcripts, which in turn can result in changes in protein production and abnormal phenotypes. For example, mice deficient in the gene encoding tristetraprolin (TTP), a ... ...

Abstract	Abnormalities in rates of mRNA decay can lead to changes in steady-state levels of transcripts, which in turn can result in changes in protein production and abnormal phenotypes. For example, mice deficient in the gene encoding tristetraprolin (TTP), a tandem CCCH zinc finger domain protein, develop a complex syndrome that includes wasting, arthritis, and myeloid hyperplasia, all secondary to elevated levels of tumor necrosis factor (TNF). This in turn reflects elevated levels of TNF mRNA, which is a direct "target" of TTP binding and TTP-promoted deadenylation and decay. Three TTP-like proteins are expressed in human and four in mice, all of which bind mRNA and control transcript decay. In contrast, the Schizosaccharomyces pombe genome contains only one TTP-like protein, named Zfs1. Microarray analysis revealed that S. pombe cells deficient in zfs1 overexpress the arz1 mRNA, which has several ideal TTP-like binding sites in its 3'-untranslated region (UTR). We used the "no message in thiamine (nmt)" repressible system, in which thiamine rapidly shuts off gene transcription, to evaluate the relative stability of the arz1 mRNA in wild-type and zfs1-deficient cells. We found that the arz1 mRNA decayed much more rapidly in the presence of endogenous zfs1 than in its absence. The nmt system also proved useful for the study of mRNA sequence elements that are essential for interactions with zfs1, which eventually results in accelerated transcript decay. These studies illustrate the utility of the S. pombe nmt system for evaluating protein-mRNA interactions that affect mRNA decay in vivo and provide an alternative to the use of transcription inhibitors or heat-sensitive polymerase promoters that are used more commonly to evaluate mRNA decay in Saccharomyces cerevesiae. We hope to use this convenient experimental system to unravel the mechanism by which TTP family members, in this and other organisms, bind to mRNAs and promote their instability.
MeSH term(s)	3' Untranslated Regions/genetics ; Amino Acid Sequence ; Molecular Sequence Data ; Protein Binding/genetics ; RNA Stability/genetics ; RNA Stability/physiology ; RNA, Messenger/genetics ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Sequence Homology, Amino Acid ; Tristetraprolin/genetics ; Tristetraprolin/physiology
Chemical Substances	3' Untranslated Regions ; RNA, Messenger ; Schizosaccharomyces pombe Proteins ; Tristetraprolin
Language	English
Publishing date	2009-02-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	1557-7988
ISSN (online)	1557-7988
DOI	10.1016/S0076-6879(08)02404-X
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Article: Discovery of synthetic penaeidin activity against antibiotic-resistant fungi.

Cuthbertson, Brandon J / Büllesbach, Erika E / Gross, Paul S

Chemical biology & drug design

2006 Volume 68, Issue 2, Page(s) 120–127

Abstract: Penaeidins are antimicrobial peptides from shrimp that are constituted by divergent classes of peptide isoforms in an individual organism. Penaeidin sequence variation suggests functional diversity in the host and promises differential activities if ... ...

Abstract	Penaeidins are antimicrobial peptides from shrimp that are constituted by divergent classes of peptide isoforms in an individual organism. Penaeidin sequence variation suggests functional diversity in the host and promises differential activities if applied to treat infections in humans. We have synthesized isoform 4 of penaeidin class 3 from the Atlantic shrimp, Litopenaeus setiferus, by native ligation using three peptide segments. Our synthesis approach led to the discovery of an irreversible side reaction that was successfully suppressed, a discovery, which has particular relevance to the synthesis of cysteine-rich peptides. The antimicrobial activity of full-length penaeidin and the N-terminal proline-rich domain of this isoform were compared with the corresponding peptides of penaeidin class 4 isoform 1 using a wide range of bacteria and fungi. New aspects of penaeidin function are reported that include activity against fungi of the phylum Basidiomycota (Cryptococcus strains), activity against fungi that are pathogenic to humans and effectiveness in the context of antibiotic resistance mechanisms (Cryptococcus and Candida spp.). The proline-rich domain of penaeidin class 4 shows the highest relative antimicrobial activity, while exhibiting no cytotoxicity to human monocytes, and therefore stands out as a potential peptide therapeutic.
MeSH term(s)	Amino Acid Sequence ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/pharmacology ; Chromatography, High Pressure Liquid ; Drug Resistance, Microbial ; Fungi/drug effects ; Microbial Sensitivity Tests ; Molecular Sequence Data ; Sequence Homology, Amino Acid ; Spectrometry, Mass, Electrospray Ionization ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Antimicrobial Cationic Peptides ; penaeidin-4 protein, Litopenaeus setiferus
Language	English
Publishing date	2006-08
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2216600-2
ISSN	1747-0285 ; 1747-0277
ISSN (online)	1747-0285
ISSN	1747-0277
DOI	10.1111/j.1747-0285.2006.00417.x
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Article: Characterization of zfs1 as an mRNA-binding and -destabilizing protein in Schizosaccharomyces pombe.

Cuthbertson, Brandon J / Liao, Yanhong / Birnbaumer, Lutz / Blackshear, Perry J

The Journal of biological chemistry

2007 Volume 283, Issue 5, Page(s) 2586–2594

Abstract: Tristetraprolin is a vertebrate CCCH tandem zinc finger protein that can bind to and destabilize certain mRNAs containing AU-rich element binding sites. zfs1 is the single gene in the fission yeast, Schizosaccharomyces pombe, that encodes a protein ... ...

Abstract	Tristetraprolin is a vertebrate CCCH tandem zinc finger protein that can bind to and destabilize certain mRNAs containing AU-rich element binding sites. zfs1 is the single gene in the fission yeast, Schizosaccharomyces pombe, that encodes a protein containing the critical features of the tristetraprolin zinc finger domain. zfs1 has been linked to pheromone signal transduction control and to the coordination of mitosis, but no biological function has been ascribed to the zfs1 protein. Through a functional genomics approach we compared transcript levels in wild-type and zfs1-deficient S. pombe strains; those elevated in the zfs1-deficient strain were examined for the presence of potential tristetraprolin-like binding sites. One such potential target transcript was encoded by arz1, a gene encoding a protein of unknown function that contains armadillo repeats. arz1 mRNA decay was inhibited in the zfs1-deficient strain when it was expressed under the control of a thiamine-repressible promoter. Mutations within one AU-rich element present in the arz1 3'-untranslated region protected this transcript from zfs1-promoted decay, whereas mutating another potential binding site had no effect. Binding assays confirmed a direct interaction between zfs1 and arz1 mRNA-based probes; this interaction was eliminated when key residues were mutated in either zfs1 zinc finger. zfs1 and its targets in S. pombe represent a useful model system for studies of zinc finger protein/AU-rich element interactions that result in mRNA decay.
MeSH term(s)	3' Untranslated Regions ; Amino Acid Sequence ; Base Sequence ; Binding Sites/genetics ; DNA Primers/genetics ; Genes, Fungal ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Phylogeny ; Protein Binding ; Protein Conformation ; RNA Stability ; RNA, Fungal/genetics ; RNA, Fungal/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Sequence Homology, Amino Acid ; Zinc Fingers/genetics
Chemical Substances	3' Untranslated Regions ; DNA Primers ; Nuclear Proteins ; RNA, Fungal ; RNA, Messenger ; Schizosaccharomyces pombe Proteins ; Zfs1 protein, S pombe
Language	English
Publishing date	2007-11-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M707154200
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Article: Characterization of zfs1 as an mRNA-binding and -destabilizing Protein in Schizosaccharomyces pombe

Cuthbertson, Brandon J / Liao, Yanhong / Birnbaumer, Lutz / Blackshear, Perry J

Journal of biological chemistry. 2008 Feb. 1, v. 283, no. 5

2008

Abstract	Tristetraprolin is a vertebrate CCCH tandem zinc finger protein that can bind to and destabilize certain mRNAs containing AU-rich element binding sites. zfs1 is the single gene in the fission yeast, Schizosaccharomyces pombe, that encodes a protein containing the critical features of the tristetraprolin zinc finger domain. zfs1 has been linked to pheromone signal transduction control and to the coordination of mitosis, but no biological function has been ascribed to the zfs1 protein. Through a functional genomics approach we compared transcript levels in wild-type and zfs1-deficient S. pombe strains; those elevated in the zfs1-deficient strain were examined for the presence of potential tristetraprolin-like binding sites. One such potential target transcript was encoded by arz1, a gene encoding a protein of unknown function that contains armadillo repeats. arz1 mRNA decay was inhibited in the zfs1-deficient strain when it was expressed under the control of a thiamine-repressible promoter. Mutations within one AU-rich element present in the arz1 3'-untranslated region protected this transcript from zfs1-promoted decay, whereas mutating another potential binding site had no effect. Binding assays confirmed a direct interaction between zfs1 and arz1 mRNA-based probes; this interaction was eliminated when key residues were mutated in either zfs1 zinc finger. zfs1 and its targets in S. pombe represent a useful model system for studies of zinc finger protein/AU-rich element interactions that result in mRNA decay.
Language	English
Dates of publication	2008-0201
Size	p. 2586-2594.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article: Diversity of the penaeidin antimicrobial peptides in two shrimp species.

Cuthbertson, Brandon J / Shepard, Eleanor F / Chapman, Robert W / Gross, Paul S

Immunogenetics

2002 Volume 54, Issue 6, Page(s) 442–445

Abstract: Penaeidins, a unique family of antimicrobial peptides (AMPs) with both proline and cysteine-rich domains, were initially identified in the hemolymph of the Pacific white shrimp, Litopenaeus vannamei. Described here are the results of an investigation of ... ...

Abstract	Penaeidins, a unique family of antimicrobial peptides (AMPs) with both proline and cysteine-rich domains, were initially identified in the hemolymph of the Pacific white shrimp, Litopenaeus vannamei. Described here are the results of an investigation of penaeidin diversity in individual shrimp from two species, L. vannamei and L. setiferus (Atlantic white shrimp). We report the discovery of a novel penaeidin class, designated penaeidin 4 present in both L. vannamei and L. setiferus, and that all penaeidin classes were expressed in a single individual. In addition, nearly all penaeidins, regardless of class, shared an identical leader sequence while differing dramatically in the remainder of the peptide. Several new class 3 isoforms were identified, as well as sequence variants of Lv3a, which differ in the 3' untranslated region. Penaeidin sequence variability (especially of class 3), within and between individuals, is not interpretable as simple allelic polymorphism and may reflect alternate transcriptional mechanisms. Penaeidins are encoded by a small number of genetic loci and are not likely representatives of a large gene family produced by whole gene duplication, but rather may be products of a multi-component locus. Based on phylogenetic analysis, penaeidins fall into three classes where 1 and 2 are combined while classes 3 and 4 remain distinct. Phylogenetic analysis indicates that all classes of penaeidin were likely present in both species prior to speciation.
MeSH term(s)	Amino Acid Sequence ; Animals ; Anti-Infective Agents/chemistry ; Decapoda (Crustacea)/genetics ; Decapoda (Crustacea)/immunology ; Genetic Variation ; Molecular Sequence Data ; Peptides ; Phylogeny ; Proteins/genetics ; Sequence Homology, Amino Acid ; Species Specificity
Chemical Substances	Anti-Infective Agents ; Peptides ; Proteins ; penaeidin 1 ; penaeidin 2 ; penaeidin 3
Language	English
Publishing date	2002-09
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	186560-2
ISSN	1432-1211 ; 0093-7711
ISSN (online)	1432-1211
ISSN	0093-7711
DOI	10.1007/s00251-002-0487-z
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Article: Solution structure of synthetic penaeidin-4 with structural and functional comparisons with penaeidin-3.

Cuthbertson, Brandon J / Yang, Yinshan / Bachère, Evelyne / Büllesbach, Erika E / Gross, Paul S / Aumelas, André

The Journal of biological chemistry

2005 Volume 280, Issue 16, Page(s) 16009–16018

Abstract: Antimicrobial peptide structure has direct implications for the complexity of functions and mechanisms of action. The penaeidin antimicrobial peptide family from shrimp is divided into multiple class designations based on primary structure. The penaeidin ...

Abstract	Antimicrobial peptide structure has direct implications for the complexity of functions and mechanisms of action. The penaeidin antimicrobial peptide family from shrimp is divided into multiple class designations based on primary structure. The penaeidin classes are not only characterized by variability in primary sequence but also by variation in target specificity and effectiveness. Whereas class 4 exhibits low isoform diversity within species and is highly conserved between species, the primary sequence of penaeidin class 3 is less conserved between species and exhibits considerable isoform diversity within species. All penaeidins, regardless of class or species, are composed of two dramatically different domains: an unconstrained proline-rich domain and a disulfide bond-stabilized cysteine-rich domain. The proline-rich domain varies in length and is generally less conserved, whereas the spacing and specific residue content of the cysteine-rich domain is more conserved. The structure of the synthetic penaeidin class 4 (PEN4-1) from Litopenaeus setiferus was analyzed using several approaches, including chemical mapping of disulfide bonds, circular dichroism analysis of secondary structural characteristics, and complete characterization of the solution structure of the peptide by proton NMR. L. setiferus PEN4-1 was then compared with the previously characterized structure of penaeidin class 3 from Litopenaeus vannamei. Moreover, the specificity of these antimicrobial peptides was examined through direct comparison of activity against a panel of microbes. The penaeidin classes differ in microbial target specificity, which correlates to variability in specific domain sequence. However, the tertiary structure of the cysteine-rich domain and indeed the overall structure of penaeidins are conserved across classes.
MeSH term(s)	Amino Acid Sequence ; Antimicrobial Cationic Peptides/chemical synthesis ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/metabolism ; Circular Dichroism ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Peptides ; Protein Structure, Tertiary ; Proteins/chemistry
Chemical Substances	Antimicrobial Cationic Peptides ; Peptides ; Proteins ; penaeidin 3 ; penaeidin-4 protein, Litopenaeus setiferus
Language	English
Publishing date	2005-02-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M412420200
Database	MEDical Literature Analysis and Retrieval System OnLINE

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