Novel families of antimicrobial peptides with multiple functions from skin of Xizang plateau frog, Nanorana parkeri

Lu, Zhenwu; Zhai, Lei; Wang, Hui; Che, Qiaolin; Wang, Duo; Feng, Feifei; Zhao, Zongmao; Yu, Haining

doi:10.1016/j.biochi.2010.01.025

Cited by 35 publications

(20 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Three kinds of AMPs (AP01357, AP00097, and AP01583) occur only in N. parkeri. AP01583 in N. parkeri serves multiple functions in defending against environmental oxidative stress and pathogenic microorganisms (25). All of the N. parkeri-specific AMPs may partially associate with ecological adaptations to its extreme environment.…”

Section: Resultsmentioning

confidence: 99%

Whole-genome sequence of the Tibetan frog Nanorana parkeri and the comparative evolution of tetrapod genomes

Sun

Xiong

Xiang

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

173

165

View full text Add to dashboard Cite

The development of efficient sequencing techniques has resulted in large numbers of genomes being available for evolutionary studies. However, only one genome is available for all amphibians, that of Xenopus tropicalis, which is distantly related from the majority of frogs. More than 96% of frogs belong to the Neobatrachia, and no genome exists for this group. This dearth of amphibian genomes greatly restricts genomic studies of amphibians and, more generally, our understanding of tetrapod genome evolution. To fill this gap, we provide the de novo genome of a Tibetan Plateau frog, Nanorana parkeri, and compare it to that of X. tropicalis and other vertebrates. This genome encodes more than 20,000 protein-coding genes, a number similar to that of Xenopus. Although the genome size of Nanorana is considerably larger than that of Xenopus (2.3 vs. 1.5 Gb), most of the difference is due to the respective number of transposable elements in the two genomes. The two frogs exhibit considerable conserved whole-genome synteny despite having diverged approximately 266 Ma, indicating a slow rate of DNA structural evolution in anurans. Multigenome synteny blocks further show that amphibians have fewer interchromosomal rearrangements than mammals but have a comparable rate of intrachromosomal rearrangements. Our analysis also identifies 11 Mb of anuran-specific highly conserved elements that will be useful for comparative genomic analyses of frogs. The Nanorana genome offers an improved understanding of evolution of tetrapod genomes and also provides a genomic reference for other evolutionary studies.de novo genome | transposable elements | chromosome rearrangement | highly conserved element T he age of genomics has ushered in opportunities to decode the history of evolution in ways unimaginable only a decade ago. More than 100 complete genomes have been sequenced and released for vertebrates. Amphibians, however, are poorly represented among these genomes. Despite the existence of more than 7,000 living species of amphibians, only the genome of Xenopus tropicalis (1) has been published. Xenopus tropicalis, however, falls outside of the Neobatrachia, which contains more than 96% of the known frog species (2). As a result, no neobatrachian genome is available for comparative analyses. Thus, this dearth of amphibian genomes greatly restricts comparative genomic studies of amphibians, and more generally, our understanding of a critical portion of tetrapod genome evolution at the major aquatic to terrestrial transition of vertebrates.Nanorana (Dicroglossidae) includes more than 20 species of frogs native to Asia (research.amnh.org/vz/herpetology/amphibia). In this genus, three species, Nanorana parkeri, Nanorana pleskei, and Nanorana ventripunctata, are endemic to the QinghaiTibetan Plateau (3). In contrast to Xenopus, which is a secondarily derived aquatic obligate, species of Nanorana exhibit the terrestrial adult lifestyle that is typical of most anurans. N. parkeri occurs at elevations ranging from 2,850 to 5,000 m. Because thi...

show abstract

Section: Resultsmentioning

confidence: 99%

Whole-genome sequence of the Tibetan frog Nanorana parkeri and the comparative evolution of tetrapod genomes

Sun

Xiong

Xiang

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

173

165

View full text Add to dashboard Cite

show abstract

“…In this study, based on previous work by Wei et al [16] and sequence alignment results, the dibasic cutting sites of Arg-Arg (R-R) and Lys-Lys (K-K) were predicted for protease cleavage to release mature C-terminal Lf-CATH1 and -2, respectively. Interestingly, although the predicted cleavage sites of arginine and lysine for amphibian cathelicidins are significantly different from those of mammals, birds and fishes, they are concordant with hundreds of ssAMPs, whose precursor structural organization also includes three parts: signal peptide, N-terminal spacer region terminating in a dibasic cutting site Lys-Arg (K-R) for trypsin-like protease cleavage, and mature ssAMPs [25]. Considering that ssAMPs and cathelicidins are both gland secretory peptides, it can be assumed that amphibian cathelicidins might also be mediated by trypsin-like proteases during the proteolysis maturation.…”

Section: Discussionmentioning

confidence: 99%

Identification and polymorphism discovery of the cathelicidins, Lf‐CATHs in ranid amphibian (Limnonectes fragilis)

Cai

Gao

et al. 2013

The FEBS Journal

Self Cite

View full text Add to dashboard Cite

To protect themselves against the invasion of microorganisms, amphibians, especially the Rana frogs, are possibly equipped with complex combinations of antimicrobial peptides (AMPs). The two major AMP families, ranid skin secretion AMPs and cathelicidins might together constitute the host innate immune system of amphibians. Cathelicidins are a group of cationic peptides found in leukocytes and epithelial cells, and they play a central role in the early innate immune defense found in virtually all species of mammals. However, they have rarely been reported from amphibians. Here, we report the identification and discovery of polymorphism cathelicidins in Limnonectes fragilis. The expression profile indicated high cathelicidin transcript levels in frog spleen, liver and kidney, but lower levels in lung, skin and stomach. According to the amphibian's unique proteolytic pattern, R125 and L121 of the prepropeptides are predicted to be the processing positions for protease to generate the mature peptides, Lf‐CATH1 and ‐2, respectively. Both consist of 30 amino acid residues, of which two were cysteines positionally conserved among a few known amphibian cathelicidins. Homology modeling analysis revealed that Lf‐CATH1 and ‐2 adopt a tertiary structure with a mostly α helix that is representative of small cationic cathelicidin family peptides. Recombinant Lf‐CATH1 (rLf‐CATH1) was produced in Escherichia coli. Synthetic Lf‐CATH1 and ‐2 displayed potent antimicrobial activities in vitro against a broad spectrum of microorganisms, including standard and clinically isolated drug‐resistant strains, while showing neglectable hemolysis and cytotoxicities.

show abstract

“…The current finding that AMPs of low anti-microbial activities usually have rather high antioxidant activities might offer firm evidence to support our claim. Our previous work about some multi-functional (antimicrobial and antioxidant) peptides from Xizang plateau frog also suggest the frog skin AMPs may participate in the frog's innate defense from different perspectives [10].…”

Section: Discussionmentioning

confidence: 99%

“…The assay was conducted as described in our previous paper [10]. Minimal inhibitory concentration (MIC) was determined in 96-well microtiter plate by a standard dilution method.…”

Section: Anti-microbial Assaymentioning

confidence: 99%

Host defense peptides in skin secretions of Odorrana tiannanensis: Proof for other survival strategy of the frog than merely anti-microbial

Feng

Huang

et al. 2012

Biochimie

Self Cite

View full text Add to dashboard Cite

Novel families of antimicrobial peptides with multiple functions from skin of Xizang plateau frog, Nanorana parkeri

Cited by 35 publications

References 21 publications

Whole-genome sequence of the Tibetan frog Nanorana parkeri and the comparative evolution of tetrapod genomes

Whole-genome sequence of the Tibetan frog Nanorana parkeri and the comparative evolution of tetrapod genomes

Identification and polymorphism discovery of the cathelicidins, Lf‐CATHs in ranid amphibian (Limnonectes fragilis)

Host defense peptides in skin secretions of Odorrana tiannanensis: Proof for other survival strategy of the frog than merely anti-microbial

Contact Info

Product

Resources

About