Heat shock protein genes (hsp20, hsp75 and hsp90) from Pieris rapae: Molecular cloning and transcription in response to parasitization by Pteromalus puparum. (20th June 2012)
- Record Type:
- Journal Article
- Title:
- Heat shock protein genes (hsp20, hsp75 and hsp90) from Pieris rapae: Molecular cloning and transcription in response to parasitization by Pteromalus puparum. (20th June 2012)
- Main Title:
- Heat shock protein genes (hsp20, hsp75 and hsp90) from Pieris rapae: Molecular cloning and transcription in response to parasitization by Pteromalus puparum
- Authors:
- Zhu, Jia‐Ying
Wu, Guo‐Xing
Ye, Gong‐Yin
Hu, Cui - Abstract:
- <abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Abstract </bold> Most molecular work on the roles of heat shock proteins (hsps) in host‐parasite interaction has focused on vertebrates, rather than invertebrates. Here the full length complementary DNA (cDNA) sequences of three hsp genes (<italic>hsp20</italic>, <italic>hsp75</italic> and <italic>hsp90</italic>) were amplified from <italic>Pieris rapae</italic>, and their transcriptional responsiveness to parasitization by the endoparasitic wasp <italic>Pteromalus puparum</italic> were investigated. The cDNA sequence analysis of <italic>hsp20</italic>, <italic>hsp75</italic> and <italic>hsp90</italic> revealed open reading frames of 531, 2 328 and 2 157 bp in length, which encode proteins with calculated molecular weights of 19.5, 75.48 and 82.7 kDa, respectively. The comparison of amino acid sequences showed that <italic>P. rapae</italic> hsp20 shared highly divergent homology to that of other insects, while hsp75 and hsp90 showed high homology to their counterparts of other species. The expression analysis indicated that these three genes were influenced in response to parasitization by <italic>P</italic>. <italic>puparum</italic>. The <italic>hsp20</italic> transcripts in parasitized pupae were higher compared to non‐parasitized pupae. The expression of <italic>hsp75</italic> and <italic>hsp90</italic> were down‐regulated following parasitization. The results<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Abstract </bold> Most molecular work on the roles of heat shock proteins (hsps) in host‐parasite interaction has focused on vertebrates, rather than invertebrates. Here the full length complementary DNA (cDNA) sequences of three hsp genes (<italic>hsp20</italic>, <italic>hsp75</italic> and <italic>hsp90</italic>) were amplified from <italic>Pieris rapae</italic>, and their transcriptional responsiveness to parasitization by the endoparasitic wasp <italic>Pteromalus puparum</italic> were investigated. The cDNA sequence analysis of <italic>hsp20</italic>, <italic>hsp75</italic> and <italic>hsp90</italic> revealed open reading frames of 531, 2 328 and 2 157 bp in length, which encode proteins with calculated molecular weights of 19.5, 75.48 and 82.7 kDa, respectively. The comparison of amino acid sequences showed that <italic>P. rapae</italic> hsp20 shared highly divergent homology to that of other insects, while hsp75 and hsp90 showed high homology to their counterparts of other species. The expression analysis indicated that these three genes were influenced in response to parasitization by <italic>P</italic>. <italic>puparum</italic>. The <italic>hsp20</italic> transcripts in parasitized pupae were higher compared to non‐parasitized pupae. The expression of <italic>hsp75</italic> and <italic>hsp90</italic> were down‐regulated following parasitization. The results indicate that hsps are involved in host‐parasitoid interactions.</p> </abstract> … (more)
- Is Part Of:
- Insect science. Volume 20:Number 2(2013:Apr.)
- Journal:
- Insect science
- Issue:
- Volume 20:Number 2(2013:Apr.)
- Issue Display:
- Volume 20, Issue 2 (2013)
- Year:
- 2013
- Volume:
- 20
- Issue:
- 2
- Issue Sort Value:
- 2013-0020-0002-0000
- Page Start:
- 183
- Page End:
- 193
- Publication Date:
- 2012-06-20
- Subjects:
- Insects -- Periodicals
Entomology -- Periodicals
595.705 - Journal URLs:
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http://firstsearch.oclc.org/dbname=ECO;journal=1672-9609;screen=available;done=referer;FSIP ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1744-7917/issues ↗
http://www.blackwell-synergy.com/loi/ins ↗
http://www.blackwell-synergy.com/openurl?genre=journal&eissn=1744-7917 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/j.1744-7917.2011.01494.x ↗
- Languages:
- English
- ISSNs:
- 1672-9609
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4516.918500
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