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Characterization and expression analysis of heat shock proteins HfHspc1 and HfHspc4 in Haemaphysalis flava ticks
In this study, the cDNAs of heat shock cognate 90 protein 1 ( HfHspc1 ) and heat shock cognate 90 protein 4 ( HfHspc4 ) from Haemaphysalis flava (Acari: Ixodidae) were obtained using the rapid amplification of cDNA ends (RACE) approach, and the expression patterns of HfHspc1 and HfHspc4 in different...
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| Published in: | Parasitology research (1987) 2024-12, Vol.123 (12), p.409 |
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| Language: | English |
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| container_issue | 12 |
| container_start_page | 409 |
| container_title | Parasitology research (1987) |
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| creator | Li, Yong Wang, Lan-Lan Feng, Li-Li Duan, De-Yong Mihaljica, Darko Cheng, Tian-Yin |
| description | In this study, the cDNAs of heat shock cognate 90 protein 1 (
HfHspc1
) and heat shock cognate 90 protein 4 (
HfHspc4
) from
Haemaphysalis flava
(Acari: Ixodidae) were obtained using the rapid amplification of cDNA ends (RACE) approach, and the expression patterns of
HfHspc1
and
HfHspc4
in different developmental stages, engorgement stages and tick organs were analyzed by qPCR. The full length of
HfHspc1
was 2411 bp, and its open reading frame (ORF) was 2196 bp, encoding a protein of 732 aa, containing five HSPC family signatures, with MEEVD motif at its extreme C-terminal. The full length of
HfHspc4
was 2800 bp, and its ORF was 2364 bp, encoding a protein of 789 aa, containing a signal peptide and five family signatures, with HEEL motif at its extreme C-terminal. The expression of
HfHspc1
and
HfHspc4
was the highest in males, while it was significantly the highest in the ovaries of fully engorged females, potentially implying the roles of these proteins in the successful digestion of blood and development of eggs. |
| doi_str_mv | 10.1007/s00436-024-08422-8 |
| format | article |
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HfHspc1
) and heat shock cognate 90 protein 4 (
HfHspc4
) from
Haemaphysalis flava
(Acari: Ixodidae) were obtained using the rapid amplification of cDNA ends (RACE) approach, and the expression patterns of
HfHspc1
and
HfHspc4
in different developmental stages, engorgement stages and tick organs were analyzed by qPCR. The full length of
HfHspc1
was 2411 bp, and its open reading frame (ORF) was 2196 bp, encoding a protein of 732 aa, containing five HSPC family signatures, with MEEVD motif at its extreme C-terminal. The full length of
HfHspc4
was 2800 bp, and its ORF was 2364 bp, encoding a protein of 789 aa, containing a signal peptide and five family signatures, with HEEL motif at its extreme C-terminal. The expression of
HfHspc1
and
HfHspc4
was the highest in males, while it was significantly the highest in the ovaries of fully engorged females, potentially implying the roles of these proteins in the successful digestion of blood and development of eggs.</description><identifier>ISSN: 0932-0113</identifier><identifier>ISSN: 1432-1955</identifier><identifier>EISSN: 1432-1955</identifier><identifier>DOI: 10.1007/s00436-024-08422-8</identifier><identifier>PMID: 39688713</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Amino Acid Sequence ; Animals ; Arthropod Proteins - genetics ; Arthropod Proteins - metabolism ; Biomedical and Life Sciences ; Biomedicine ; Developmental stages ; DNA, Complementary - genetics ; Engorgement ; Female ; Gene Expression Profiling ; Haemaphysalis flava ; Heat shock proteins ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - metabolism ; Immunology ; Ixodidae - genetics ; Ixodidae - metabolism ; Male ; Medical Microbiology ; Microbiology ; Molecular Sequence Data ; Open reading frames ; Phylogeny ; Proteins ; Real-Time Polymerase Chain Reaction ; Sequence Analysis, DNA</subject><ispartof>Parasitology research (1987), 2024-12, Vol.123 (12), p.409</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2024 Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.</rights><rights>Copyright Springer Nature B.V. 2024</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39688713$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Yong</creatorcontrib><creatorcontrib>Wang, Lan-Lan</creatorcontrib><creatorcontrib>Feng, Li-Li</creatorcontrib><creatorcontrib>Duan, De-Yong</creatorcontrib><creatorcontrib>Mihaljica, Darko</creatorcontrib><creatorcontrib>Cheng, Tian-Yin</creatorcontrib><title>Characterization and expression analysis of heat shock proteins HfHspc1 and HfHspc4 in Haemaphysalis flava ticks</title><title>Parasitology research (1987)</title><addtitle>Parasitol Res</addtitle><addtitle>Parasitol Res</addtitle><description>In this study, the cDNAs of heat shock cognate 90 protein 1 (
HfHspc1
) and heat shock cognate 90 protein 4 (
HfHspc4
) from
Haemaphysalis flava
(Acari: Ixodidae) were obtained using the rapid amplification of cDNA ends (RACE) approach, and the expression patterns of
HfHspc1
and
HfHspc4
in different developmental stages, engorgement stages and tick organs were analyzed by qPCR. The full length of
HfHspc1
was 2411 bp, and its open reading frame (ORF) was 2196 bp, encoding a protein of 732 aa, containing five HSPC family signatures, with MEEVD motif at its extreme C-terminal. The full length of
HfHspc4
was 2800 bp, and its ORF was 2364 bp, encoding a protein of 789 aa, containing a signal peptide and five family signatures, with HEEL motif at its extreme C-terminal. The expression of
HfHspc1
and
HfHspc4
was the highest in males, while it was significantly the highest in the ovaries of fully engorged females, potentially implying the roles of these proteins in the successful digestion of blood and development of eggs.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Arthropod Proteins - genetics</subject><subject>Arthropod Proteins - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Developmental stages</subject><subject>DNA, Complementary - genetics</subject><subject>Engorgement</subject><subject>Female</subject><subject>Gene Expression Profiling</subject><subject>Haemaphysalis flava</subject><subject>Heat shock proteins</subject><subject>Heat-Shock Proteins - genetics</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Immunology</subject><subject>Ixodidae - genetics</subject><subject>Ixodidae - metabolism</subject><subject>Male</subject><subject>Medical Microbiology</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Open reading frames</subject><subject>Phylogeny</subject><subject>Proteins</subject><subject>Real-Time Polymerase Chain Reaction</subject><subject>Sequence Analysis, DNA</subject><issn>0932-0113</issn><issn>1432-1955</issn><issn>1432-1955</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNpdkU1PwzAMhiMEYmPwBzigSFy4FPLVJD2iCRjSJC5wjrw0Zd26ttQdYvx6Ah1C4mRbfmz59UvIOWfXnDFzg4wpqRMmVMKsEiKxB2TMlRQJz9L0kIxZFnPGuRyRE8QVY9xopY7JSGbaWsPlmLTTJXTg-9CVn9CXTU2hzmn4aLuAOJRQ7bBE2hR0GaCnuGz8mrZd04eyRjorZth6_jM25IqWNZ1B2EC73CFUcbao4B1oX_o1npKjAioMZ_s4IS_3d8_TWTJ_enic3s6TlgtrE5MbpcCkUtic6dz6VEuzMN74zOQcrC5yyLTJo55FqpQXLDCbGh0Agi-kkBNyNeyNl75tA_ZuU6IPVQV1aLboJFc6E6mx3-jlP3TVbLuoe6BUppXVkbrYU9vFJuSu7coNdDv3-8sIyAHA2KpfQ_e3hjP37ZgbHHPRMffjmLPyC3T2hjQ</recordid><startdate>20241217</startdate><enddate>20241217</enddate><creator>Li, Yong</creator><creator>Wang, Lan-Lan</creator><creator>Feng, Li-Li</creator><creator>Duan, De-Yong</creator><creator>Mihaljica, Darko</creator><creator>Cheng, Tian-Yin</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20241217</creationdate><title>Characterization and expression analysis of heat shock proteins HfHspc1 and HfHspc4 in Haemaphysalis flava ticks</title><author>Li, Yong ; Wang, Lan-Lan ; Feng, Li-Li ; Duan, De-Yong ; Mihaljica, Darko ; Cheng, Tian-Yin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1288-7d744a75328d06d8c5637b7c7c97d1a86fda967d644b544c20e08576eaaecf323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Arthropod Proteins - genetics</topic><topic>Arthropod Proteins - metabolism</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Developmental stages</topic><topic>DNA, Complementary - genetics</topic><topic>Engorgement</topic><topic>Female</topic><topic>Gene Expression Profiling</topic><topic>Haemaphysalis flava</topic><topic>Heat shock proteins</topic><topic>Heat-Shock Proteins - genetics</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Immunology</topic><topic>Ixodidae - genetics</topic><topic>Ixodidae - metabolism</topic><topic>Male</topic><topic>Medical Microbiology</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Open reading frames</topic><topic>Phylogeny</topic><topic>Proteins</topic><topic>Real-Time Polymerase Chain Reaction</topic><topic>Sequence Analysis, DNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Yong</creatorcontrib><creatorcontrib>Wang, Lan-Lan</creatorcontrib><creatorcontrib>Feng, Li-Li</creatorcontrib><creatorcontrib>Duan, De-Yong</creatorcontrib><creatorcontrib>Mihaljica, Darko</creatorcontrib><creatorcontrib>Cheng, Tian-Yin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Parasitology research (1987)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Yong</au><au>Wang, Lan-Lan</au><au>Feng, Li-Li</au><au>Duan, De-Yong</au><au>Mihaljica, Darko</au><au>Cheng, Tian-Yin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and expression analysis of heat shock proteins HfHspc1 and HfHspc4 in Haemaphysalis flava ticks</atitle><jtitle>Parasitology research (1987)</jtitle><stitle>Parasitol Res</stitle><addtitle>Parasitol Res</addtitle><date>2024-12-17</date><risdate>2024</risdate><volume>123</volume><issue>12</issue><spage>409</spage><pages>409-</pages><issn>0932-0113</issn><issn>1432-1955</issn><eissn>1432-1955</eissn><abstract>In this study, the cDNAs of heat shock cognate 90 protein 1 (
HfHspc1
) and heat shock cognate 90 protein 4 (
HfHspc4
) from
Haemaphysalis flava
(Acari: Ixodidae) were obtained using the rapid amplification of cDNA ends (RACE) approach, and the expression patterns of
HfHspc1
and
HfHspc4
in different developmental stages, engorgement stages and tick organs were analyzed by qPCR. The full length of
HfHspc1
was 2411 bp, and its open reading frame (ORF) was 2196 bp, encoding a protein of 732 aa, containing five HSPC family signatures, with MEEVD motif at its extreme C-terminal. The full length of
HfHspc4
was 2800 bp, and its ORF was 2364 bp, encoding a protein of 789 aa, containing a signal peptide and five family signatures, with HEEL motif at its extreme C-terminal. The expression of
HfHspc1
and
HfHspc4
was the highest in males, while it was significantly the highest in the ovaries of fully engorged females, potentially implying the roles of these proteins in the successful digestion of blood and development of eggs.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>39688713</pmid><doi>10.1007/s00436-024-08422-8</doi></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0932-0113 |
| ispartof | Parasitology research (1987), 2024-12, Vol.123 (12), p.409 |
| issn | 0932-0113 1432-1955 1432-1955 |
| language | eng |
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| source | Springer Nature |
| subjects | Amino Acid Sequence Animals Arthropod Proteins - genetics Arthropod Proteins - metabolism Biomedical and Life Sciences Biomedicine Developmental stages DNA, Complementary - genetics Engorgement Female Gene Expression Profiling Haemaphysalis flava Heat shock proteins Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism Immunology Ixodidae - genetics Ixodidae - metabolism Male Medical Microbiology Microbiology Molecular Sequence Data Open reading frames Phylogeny Proteins Real-Time Polymerase Chain Reaction Sequence Analysis, DNA |
| title | Characterization and expression analysis of heat shock proteins HfHspc1 and HfHspc4 in Haemaphysalis flava ticks |
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