scholarly journals The non-specific lipid transfer protein N5 of Medicago truncatula is implicated in epidermal stages of rhizobium-host interaction

2012 ◽  
Vol 12 (1) ◽  
pp. 233 ◽  
Author(s):  
Youry Pii ◽  
Barbara Molesini ◽  
Simona Masiero ◽  
Tiziana Pandolfini
Keyword(s):  
Medicago Truncatula ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Host Interaction ◽  
Specific Lipid

scholarly journals Structural Characterization of Act c 10.0101 and Pun g 1.0101—Allergens from the Non-Specific Lipid Transfer Protein Family

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 256
Author(s):  
Andrea O’Malley ◽  
Swanandi Pote ◽  
Ivana Giangrieco ◽  
Lisa Tuppo ◽  
Anna Gawlicka-Chruszcz ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Lipid Transfer Protein ◽  
Mass Spectrometry Analysis ◽  
Lipid Transfer ◽  
Helical Structures ◽  
Spectrometry Analysis ◽  
X Ray Crystallography ◽  
Transfer Protein ◽  
Specific Lipid

(1) Background: Non-specific lipid transfer proteins (nsLTPs), which belong to the prolamin superfamily, are potent allergens. While the biological role of LTPs is still not well understood, it is known that these proteins bind lipids. Allergen nsLTPs are characterized by significant stability and resistance to digestion. (2) Methods: nsLTPs from gold kiwifruit (Act c 10.0101) and pomegranate (Pun g 1.0101) were isolated from their natural sources and structurally characterized using X-ray crystallography (3) Results: Both proteins crystallized and their crystal structures were determined. The proteins have a very similar overall fold with characteristic compact, mainly α-helical structures. The C-terminal sequence of Act c 10.0101 was updated based on our structural and mass spectrometry analysis. Information on proteins’ sequences and structures was used to estimate the risk of cross-reactive reactions between Act c 10.0101 or Pun g 1.0101 and other allergens from this family of proteins. (4) Conclusions: Structural studies indicate a conformational flexibility of allergens from the nsLTP family and suggest that immunoglobulin E binding to some surface regions of these allergens may depend on ligand binding. Both Act c 10.0101 and Pun g 1.0101 are likely to be involved in cross-reactive reactions involving other proteins from the nsLTP family.

Non-specific Lipid Transfer Protein (Can s 3) Is a Relevant Cannabis Allergen in North America

2021 ◽  
Vol 147 (2) ◽  
pp. AB171
Author(s):  
Henry Morelli ◽  
Cathy Thorpe ◽  
Ine Decuyper ◽  
Cali Loblundo ◽  
Khaldon Abbas ◽  
...  
Keyword(s):  
North America ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Specific Lipid

scholarly journals High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings

Structure ◽  
1995 ◽  
Vol 3 (2) ◽  
pp. 189-199 ◽  
Author(s):  
Dong Hae Shin ◽  
Jae Young Lee ◽  
Kwang Yeon Hwang ◽  
Kyeong Kyu Kim ◽  
Se Won Suh
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Maize Seedlings ◽  
Transfer Protein ◽  
Specific Lipid

scholarly journals Early transcriptomic response of Alnus glutinosa to Frankia alni symbiont, an upregulated nsLTP (non-specific Lipid Transfer Protein) is implicated in early and late stages of symbiosis

2021 ◽  
Author(s):  
Melanie Gasser ◽  
Nicole Alloisio ◽  
Pascale Fournier ◽  
Severine Balmand ◽  
Ons Kharrat ◽  
...  
Keyword(s):  
Root Hair ◽  
Lipid Transfer Protein ◽  
Alnus Glutinosa ◽  
Lipid Transfer ◽  
Transcriptomic Response ◽  
Transfer Protein ◽  
Root Hair Deformation ◽  
Frankia Alni ◽  
Late Stages ◽  
Specific Lipid

The response of Alnus glutinosa to Frankia alni is complex with several sequential physiological modifications that include calcium spiking, root hair deformation, penetration, induction of primordium, formation and growth of nodule. A transcriptomic study of seedlings in hydroponics after early contact (2.5 days) with Frankia alni, either with a culture supernatant or with living cells separated from the roots by a dialysis membrane, permitted to identify plant genes which expression level was modified upon early contact with Frankia. Forty-two genes were significantly up-regulated in both experiments, most of them encoding biological processes such as oxidative stress or response to stimuli. Among them, the most upregulated gene was a non-specific lipid transfer protein encoding gene with a fold change of 141. This nsLTP was found to increase Frankia nitrogen fixation at sub-lethal concentration. Interestingly, it was immunolocalized to a region of the deformed root hair at an early infection stage and later in nodules, it was localized around bacterial vesicles suggesting a role in early and late stages of symbiosis.

scholarly journals The Medicago truncatula N5 Gene Encoding a Root-Specific Lipid Transfer Protein Is Required for the Symbiotic Interaction with Sinorhizobium meliloti

2009 ◽  
Vol 22 (12) ◽  
pp. 1577-1587 ◽  
Author(s):  
Youry Pii ◽  
Alessandra Astegno ◽  
Elisa Peroni ◽  
Massimo Zaccardelli ◽  
Tiziana Pandolfini ◽  
...  
Keyword(s):  
Medicago Truncatula ◽  
Sinorhizobium Meliloti ◽  
Lipid Transfer Protein ◽  
Symbiotic Association ◽  
Lipid Transfer ◽  
Symbiotic Interaction ◽  
Transgenic Roots ◽  
Transfer Protein ◽  
Small Proteins

The Medicago truncatula N5 gene is induced in roots after Sinorhizobium meliloti infection and it codes for a putative lipid transfer protein (LTP), a family of plant small proteins capable of binding and transferring lipids between membranes in vitro. Various biological roles for plant LTP in vivo have been proposed, including defense against pathogens and modulation of plant development. The aim of this study was to shed light on the role of MtN5 in the symbiotic interaction between M. truncatula and S. meliloti. MtN5 cDNA was cloned and the mature MtN5 protein expressed in Escherichia coli. The lipid binding capacity and antimicrobial activity of the recombinant MtN5 protein were tested in vitro. MtN5 showed the capacity to bind lysophospholipids and to inhibit M. truncatula pathogens and symbiont growth in vitro. Furthermore, MtN5 was upregulated in roots after infection with either the fungal pathogen Fusarium semitectum or the symbiont S. meliloti. Upon S. meliloti infection, MtN5 was induced starting from 1 day after inoculation (dpi). It reached the highest concentration at 3 dpi and it was localized in the mature nodules. MtN5-silenced roots were impaired in nodulation, showing a 50% of reduction in the number of nodules compared with control roots. On the other hand, transgenic roots overexpressing MtN5 developed threefold more nodules with respect to control roots. Here, we demonstrate that MtN5 possesses biochemical features typical of LTP and that it is required for the successful symbiotic association between M. truncatula and S. meliloti.

The non-specific lipid transfer protein, Ara h 9, is an important allergen in peanut

2009 ◽  
Vol 39 (9) ◽  
pp. 1427-1437 ◽  
Author(s):  
I. Lauer ◽  
N. Dueringer ◽  
S. Pokoj ◽  
S. Rehm ◽  
G. Zoccatelli ◽  
...  
Keyword(s):  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Specific Lipid

LOCALIZATION AND HORMONAL REGULATION OF THE NON-SPECIFIC LIPID TRANSFER PROTEIN (STEROL CARRIER PROTEIN2) IN THE RAT TESTIS

1986 ◽  
Vol 109 (3) ◽  
pp. R13-R16 ◽  
Author(s):  
M. van Noort ◽  
F.F.G. Rommerts ◽  
A. van Amerongen ◽  
K.W.A. Wirtz
Keyword(s):  
Luteinizing Hormone ◽  
Hormonal Regulation ◽  
Leydig Cells ◽  
Lipid Transfer Protein ◽  
Cell Fractionation ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Germinal Cells ◽  
Specific Lipid ◽  
Testis Tissue

ABSTRACT In testis tissue from mature rats the non-specific lipid transfer protein (nsLTP), also called sterol carrier protein2 (SCP2), is concentrated in the Leydig cells and cannot be detected in Sertoli cells or germinal cells. Conclusions were reached after cell fractionation studies with normal testis tissue and after selective destruction of Leydig cells or germinal cells in vivo. The amount of nsLTP (SCP2) in testis tissue increased twofold 48 h after two daily injections of human chorionic gonadotrophin (100 i.u., s.c.) and decreased twofold after plasma luteinizing hormone levels were suppressed to almost undetectable levels with silicone elastomer implants containing testosterone. The specific localization in the Leydig cells and the luteinizing hormone-dependent cellular concentration of nsLTP/SCP2 support the possibility that this protein could play a role in the regulation of steroidogenesis by regulating the availability of cholesterol for the P450 side-chain cleavage enzyme in the mitochondria of Leydig cells.

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