Transduction of Proteins into Leishmania Tarentolae by Formation of Non‐Covalent Complexes With Cell‐Penetrating Peptides. Issue 2 (February 2014)
- Record Type:
- Journal Article
- Title:
- Transduction of Proteins into Leishmania Tarentolae by Formation of Non‐Covalent Complexes With Cell‐Penetrating Peptides. Issue 2 (February 2014)
- Main Title:
- Transduction of Proteins into Leishmania Tarentolae by Formation of Non‐Covalent Complexes With Cell‐Penetrating Peptides
- Authors:
- Keller, Andrea‐Anneliese
Breitling, Reinhard
Hemmerich, Peter
Kappe, Katarina
Braun, Maria
Wittig, Berith
Schaefer, Buerk
Lorkowski, Stefan
Reissmann, Siegmund - Abstract:
- <abstract abstract-type="main" xml:lang="en"> <title>ABSTRACT</title> <sec id="jcb24654-sec-0001" sec-type="section"> <p>Cell‐penetrating peptides (CPPs) are used to transport peptides, proteins, different types of ribonucleic acids (or mimics of these molecules), and DNA into live cells, both plant and mammalian. Leishmania belongs to the class of protozoa having, in comparison to mammalian cells, a different lipid composition of the membrane, proteoglycans on the surface, and signal pathways. We investigated the uptake of two different and easily detectable proteins into the non‐pathogenic strain <italic>Leishmania tarentolae</italic>. From the large number of CPPs available, six and a histone were chosen specifically for their ability to form non‐covalent complexes. For <italic>Leishmania</italic> we used the enzyme β‐galactosidase and fluorescent labeled bovine serum albumin as cargoes. The results are compared to similar internalization studies using mammalian cells [Mussbach et al., <xref ref-type="link" rid="jcb24654-bib-0040">2011a</xref>]. <italic>Leishmania</italic> cells can degrade CPPs by a secreted and membrane‐bound chymotrypsin‐like protease. Both cargo proteins were internalized with sufficient efficiency and achieved intramolecular concentrations similar to mammalian cells. The transport efficiencies of the CPPs differed from each other, and showed a different rank order for both cargoes. The intracellular distribution of fluorescent‐labeled bovine serum<abstract abstract-type="main" xml:lang="en"> <title>ABSTRACT</title> <sec id="jcb24654-sec-0001" sec-type="section"> <p>Cell‐penetrating peptides (CPPs) are used to transport peptides, proteins, different types of ribonucleic acids (or mimics of these molecules), and DNA into live cells, both plant and mammalian. Leishmania belongs to the class of protozoa having, in comparison to mammalian cells, a different lipid composition of the membrane, proteoglycans on the surface, and signal pathways. We investigated the uptake of two different and easily detectable proteins into the non‐pathogenic strain <italic>Leishmania tarentolae</italic>. From the large number of CPPs available, six and a histone were chosen specifically for their ability to form non‐covalent complexes. For <italic>Leishmania</italic> we used the enzyme β‐galactosidase and fluorescent labeled bovine serum albumin as cargoes. The results are compared to similar internalization studies using mammalian cells [Mussbach et al., <xref ref-type="link" rid="jcb24654-bib-0040">2011a</xref>]. <italic>Leishmania</italic> cells can degrade CPPs by a secreted and membrane‐bound chymotrypsin‐like protease. Both cargo proteins were internalized with sufficient efficiency and achieved intramolecular concentrations similar to mammalian cells. The transport efficiencies of the CPPs differed from each other, and showed a different rank order for both cargoes. The intracellular distribution of fluorescent‐labeled bovine serum albumin showed highest concentrations in the nucleus and kinetoplast. <italic>Leishmania</italic> are susceptible to high concentrations of some CPPs, although comparably dissimilar to mammalian cells. MPG‐peptides are more cytotoxic in <italic>Leishmania</italic> than in mammalian cells, acting as antimicrobial peptides. Our results contribute to a better understanding of molecular interactions in <italic>Leishmania</italic> cells and possibly to new treatments of leishmaniasis. J. Cell. Biochem. 115: 243–252, 2014. © 2013 Wiley Periodicals, Inc.</p> </sec> </abstract> … (more)
- Is Part Of:
- Journal of cellular biochemistry. Volume 115:Issue 2(2014:Feb.)
- Journal:
- Journal of cellular biochemistry
- Issue:
- Volume 115:Issue 2(2014:Feb.)
- Issue Display:
- Volume 115, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 115
- Issue:
- 2
- Issue Sort Value:
- 2014-0115-0002-0000
- Page Start:
- 243
- Page End:
- 252
- Publication Date:
- 2014-02
- Subjects:
- Cytochemistry -- Periodicals
572 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-4644 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/jcb.24654 ↗
- Languages:
- English
- ISSNs:
- 0730-2312
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4955.010000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3090.xml