scholarly journals Activities of Temporin Family Peptides against the Chytrid Fungus (Batrachochytrium dendrobatidis) Associated with Global Amphibian Declines

2003 ◽  
Vol 47 (3) ◽  
pp. 1157-1160 ◽  
Author(s):  
Louise A. Rollins-Smith ◽  
Cynthia Carey ◽  
J. Michael Conlon ◽  
Laura K. Reinert ◽  
Jennifer K. Doersam ◽  
...  
Keyword(s):  
Amino Acid ◽  
Growth Inhibition ◽  
Amino Acid Substitution ◽  
Batrachochytrium Dendrobatidis ◽  
Helical Structure ◽  
Amphibian Declines ◽  
Chytrid Fungus ◽  
Wasp Venom ◽  
Growth Differences ◽  
Temporin A

ABSTRACT Temporin A and structurally related peptides produced in amphibian dermal granular glands and in wasp venom were tested for growth inhibition of Batrachochytrium dendrobatidis, a pathogen associated with global amphibian declines. Two natural amphibian temporins, a wasp temporin, and six synthetic analogs effectively inhibited growth. Differences in potency due to amino acid substitution suggest that ability to penetrate membranes and form an α-helical structure is important for their effectiveness against this pathogen.

scholarly journals Impacts of thermal mismatches on chytrid fungus Batrachochytrium dendrobatidis prevalence are moderated by life stage, body size, elevation and latitude

2018 ◽  
Author(s):  
Jeremy M. Cohen ◽  
Taegan A. McMahon ◽  
Chloe Ramsay ◽  
Elizabeth A. Roznik ◽  
Erin L. Sauer ◽  
...  
Keyword(s):  
Body Size ◽  
Batrachochytrium Dendrobatidis ◽  
Global Climate ◽  
Global Analysis ◽  
Life Stage ◽  
Conservation Status ◽  
Amphibian Declines ◽  
Lower Latitude ◽  
Infection Prevalence ◽  
Chytrid Fungus

AbstractGlobal climate change is increasing the frequency of unpredictable weather conditions; however, it remains unclear how species-level and geographic factors, including body size and latitude, moderate impacts of unusually warm or cool temperatures on disease. Because larger hosts and lower-latitude hosts generally have slower acclimation times, we hypothesized that their disease susceptibility increases under “thermal mismatches”, or differences between baseline climate and the temperature during surveying. Here, we examined how thermal mismatches interact with body size, life stage, habitat, latitude, elevation, phylogeny, and IUCN conservation status to predict infection prevalence of the chytrid fungus Batrachochytrium dendrobatidis (Bd) in a global analysis of 38,967 amphibian hosts. As hypothesized, we found that the susceptibility of larger hosts and hosts from lower latitudes was strongly influenced by thermal mismatches. Furthermore, hosts of conservation concern are more susceptible than others following thermal mismatches, suggesting that thermal mismatches might have contributed to recent amphibian declines.Data Accessibility StatementShould the manuscript be accepted, the data supporting the results will be archived in an appropriate public repository such as Dryad or Figshare and the data DOI will be included at the end of the article.

scholarly journals PRESENCE AND PREVALENCE OF BD (BATRACHOCHYTRIUM DENDROBATIDIS) IN CENTRAL PENNSYLVANIAN WOODLAND VERNAL POOLS

2016 ◽  
pp. 11-14
Author(s):  
Kristen S. Coury ◽  
Brennan A. Neal ◽  
Michael J. Shin ◽  
Erik D. Lindquist
Keyword(s):  
Ambient Temperature ◽  
Batrachochytrium Dendrobatidis ◽  
Vernal Pools ◽  
Amphibian Declines ◽  
Late Winter ◽  
Chytrid Fungus ◽  
Migration Timing ◽  
Anuran Species ◽  
Central Pennsylvania ◽  
Woodland Vernal Pools

Batrachochytrium dendrobatidis (Bd), a virulent chytrid fungus responsible for dramatic amphibian declines, has been detected in the northwestern and southeastern regions of Pennsylvania. However, little environmental Bd testing has been performed in central Pennsylvania, particularly in the unique and speciose habitats of woodland vernal pools. Our study included sampling in four vernal pools over a period of three months during amphibian breeding periods. Skin swabs were taken from three caudate and two anuran species, during the course of late winter and spring migrations (n = 143). Low Bd zoospore equivalent loads were detected in only a few individuals, in three of the five species but in all four vernal pools sampled. No significant trends were seen between zoospore loads and ambient temperature or migration timing across the species sampled.

Activity of antimicrobial skin peptides from ranid frogs against Batrachochytrium dendrobatidis, the chytrid fungus associated with global amphibian declines

2002 ◽  
Vol 26 (5) ◽  
pp. 471-479 ◽  
Author(s):  
Louise A Rollins-Smith ◽  
Cynthia Carey ◽  
Joyce Longcore ◽  
Jennifer K Doersam ◽  
Angela Boutte ◽  
...  
Keyword(s):  
Batrachochytrium Dendrobatidis ◽  
Amphibian Declines ◽  
Chytrid Fungus

Hubsm: A Novel Amino Acid Substitution Matrix for Comparing Hub Proteins

2017 ◽  
Vol 7 (8) ◽  
pp. 212
Author(s):  
Renganayaki G. ◽  
Achuthsankar S. Nair
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Low Complexity ◽  
Database Search ◽  
Substitution Matrix ◽  
Compositional Bias ◽  
Sequence Alignments ◽  
Amino Acid Substitution Matrix ◽  
Alignment Algorithms ◽  
Hub Proteins

Sequence alignment algorithms and  database search methods use BLOSUM and PAM substitution matrices constructed from general proteins. These de facto matrices are not optimal to align sequences accurately, for the proteins with markedly different compositional bias in the amino acid.   In this work, a new amino acid substitution matrix is calculated for the disorder and low complexity rich region of Hub proteins, based on residue characteristics. Insights into the amino acid background frequencies and the substitution scores obtained from the Hubsm unveils the  residue substitution patterns which differs from commonly used scoring matrices .When comparing the Hub protein sequences for detecting homologs,  the use of this Hubsm matrix yields better results than PAM and BLOSUM matrices. Usage of Hubsm matrix can be optimal in database search and for the construction of more accurate sequence alignments of Hub proteins.

scholarly journals A large compressibility change of protein induced by a single amino acid substitution

1996 ◽  
Vol 5 (3) ◽  
pp. 542-545 ◽  
Author(s):  
Kunihiko Gekko ◽  
Youjiro Tamura ◽  
Eiji Ohmae ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid

scholarly journals Primary- and secondary-structural analysis of a unique prokaryotic metallothionein from a Synechococcus sp. cyanobacterium

1988 ◽  
Vol 251 (3) ◽  
pp. 691-699 ◽  
Author(s):  
R W Olafson ◽  
W D McCubbin ◽  
C M Kay
Keyword(s):  
Amino Acid ◽  
Metal Binding ◽  
Helical Structure ◽  
Basic Amino Acid ◽  
Cysteine Residues ◽  
Amino Acid Residues ◽  
C Terminus ◽  
Empirical Relations ◽  
Heavy Metal Binding ◽  
Synechococcus Sp

Biochemical and physiological studies of Synechococcus cyanobacteria have indicated the presence of a low-Mr heavy-metal-binding protein with marked similarity to eukaryotic metallothioneins (MTs). We report here the characterization of a Synechococcus prokaryotic MT isolated by gel-permeation and reverse-phase chromatography. The large number of variants of this molecule found during chromatographic separation could not be attributed to the presence of major isoproteins as assessed by amino acid analysis and amino acid sequencing of isoforms. Two of the latter were shown to have identical primary structures that differed substantially from the well-described eukaryotic MTs. In addition to six long-chain aliphatic residues, two aromatic residues were found adjacent to one another near the centre of the molecule, making this the most hydrophobic MT to be described. Other unusual features included a pair of histidine residues located in repeating Gly-His-Thr-Gly sequences near the C-terminus and a complete lack of association of hydroxylated residues with cysteine residues, as is commonly found in eukaryotes. Similarly, aside from a single lysine residue, no basic amino acid residues were found adjacent to cysteine residues in the sequence. Most importantly, sequence alignment analyses with mammalian, invertebrate and fungal MT sequences showed no statistically significant homology aside from the presence of Cys-Xaa-Cys structures common to all MTs. On the other hand, like other MTs, the prokaryotic molecule appears to be free of alpha-helical structure but has a considerable amount of beta-structure, as predicted by both c.d. measurements and the Chou & Fasman empirical relations. Considered together, these data suggested that some similarity between the metal-thiolate clusters of the prokaryote and eukaryote MTs may exist.

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