---
_id: '14776'
abstract:
- lang: eng
  text: Soluble chaperones residing in the endoplasmic reticulum (ER) play vitally
    important roles in folding and quality control of newly synthesized proteins that
    transiently pass through the ER en route to their final destinations. These soluble
    residents of the ER are themselves endowed with an ER retrieval signal that enables
    the cell to bring the escaped residents back from the Golgi. Here, by using purified
    proteins, we showed that Nicotiana tabacum phytaspase, a plant aspartate-specific
    protease, introduces two breaks at the C-terminus of the N. tabacum ER resident
    calreticulin-3. These cleavages resulted in removal of either a dipeptide or a
    hexapeptide from the C-terminus of calreticulin-3 encompassing part or all of
    the ER retrieval signal. Consistently, expression of the calreticulin-3 derivative
    mimicking the phytaspase cleavage product in Nicotiana benthamiana cells demonstrated
    loss of the ER accumulation of the protein. Notably, upon its escape from the
    ER, calreticulin-3 was further processed by an unknown protease(s) to generate
    the free N-terminal (N) domain of calreticulin-3, which was ultimately secreted
    into the apoplast. Our study thus identified a specific proteolytic enzyme capable
    of precise detachment of the ER retrieval signal from a plant ER resident protein,
    with implications for the further fate of the escaped resident.
acknowledgement: "We thank C.U.T. Hellen for critically reading the manuscript. The
  MALDI MS facility and CLSM became available to us in the framework of Moscow State
  University Development Programs PNG 5.13 and PNR 5.13.\r\nThis work was funded by
  the Russian Science Foundation, grant numbers 19-14-00010 and 22-14-00071."
article_number: '16527'
article_processing_charge: Yes
article_type: original
author:
- first_name: Anastasiia
  full_name: Teplova, Anastasiia
  id: e3736151-106c-11ec-b916-c2558e2762c6
  last_name: Teplova
- first_name: Artemii A.
  full_name: Pigidanov, Artemii A.
  last_name: Pigidanov
- first_name: Marina V.
  full_name: Serebryakova, Marina V.
  last_name: Serebryakova
- first_name: Sergei A.
  full_name: Golyshev, Sergei A.
  last_name: Golyshev
- first_name: Raisa A.
  full_name: Galiullina, Raisa A.
  last_name: Galiullina
- first_name: Nina V.
  full_name: Chichkova, Nina V.
  last_name: Chichkova
- first_name: Andrey B.
  full_name: Vartapetian, Andrey B.
  last_name: Vartapetian
citation:
  ama: Teplova A, Pigidanov AA, Serebryakova MV, et al. Phytaspase Is capable of detaching
    the endoplasmic reticulum retrieval signal from tobacco calreticulin-3. <i>International
    Journal of Molecular Sciences</i>. 2023;24(22). doi:<a href="https://doi.org/10.3390/ijms242216527">10.3390/ijms242216527</a>
  apa: Teplova, A., Pigidanov, A. A., Serebryakova, M. V., Golyshev, S. A., Galiullina,
    R. A., Chichkova, N. V., &#38; Vartapetian, A. B. (2023). Phytaspase Is capable
    of detaching the endoplasmic reticulum retrieval signal from tobacco calreticulin-3.
    <i>International Journal of Molecular Sciences</i>. MDPI. <a href="https://doi.org/10.3390/ijms242216527">https://doi.org/10.3390/ijms242216527</a>
  chicago: Teplova, Anastasiia, Artemii A. Pigidanov, Marina V. Serebryakova, Sergei
    A. Golyshev, Raisa A. Galiullina, Nina V. Chichkova, and Andrey B. Vartapetian.
    “Phytaspase Is Capable of Detaching the Endoplasmic Reticulum Retrieval Signal
    from Tobacco Calreticulin-3.” <i>International Journal of Molecular Sciences</i>.
    MDPI, 2023. <a href="https://doi.org/10.3390/ijms242216527">https://doi.org/10.3390/ijms242216527</a>.
  ieee: A. Teplova <i>et al.</i>, “Phytaspase Is capable of detaching the endoplasmic
    reticulum retrieval signal from tobacco calreticulin-3,” <i>International Journal
    of Molecular Sciences</i>, vol. 24, no. 22. MDPI, 2023.
  ista: Teplova A, Pigidanov AA, Serebryakova MV, Golyshev SA, Galiullina RA, Chichkova
    NV, Vartapetian AB. 2023. Phytaspase Is capable of detaching the endoplasmic reticulum
    retrieval signal from tobacco calreticulin-3. International Journal of Molecular
    Sciences. 24(22), 16527.
  mla: Teplova, Anastasiia, et al. “Phytaspase Is Capable of Detaching the Endoplasmic
    Reticulum Retrieval Signal from Tobacco Calreticulin-3.” <i>International Journal
    of Molecular Sciences</i>, vol. 24, no. 22, 16527, MDPI, 2023, doi:<a href="https://doi.org/10.3390/ijms242216527">10.3390/ijms242216527</a>.
  short: A. Teplova, A.A. Pigidanov, M.V. Serebryakova, S.A. Golyshev, R.A. Galiullina,
    N.V. Chichkova, A.B. Vartapetian, International Journal of Molecular Sciences
    24 (2023).
date_created: 2024-01-10T09:24:35Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-01-10T13:41:10Z
day: '01'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.3390/ijms242216527
external_id:
  isi:
  - '001113792600001'
  pmid:
  - '38003717'
file:
- access_level: open_access
  checksum: 4df7d206ba022b7f54eff1f0aec1659a
  content_type: application/pdf
  creator: dernst
  date_created: 2024-01-10T13:39:42Z
  date_updated: 2024-01-10T13:39:42Z
  file_id: '14791'
  file_name: 2023_IJMS_Teplova.pdf
  file_size: 2637784
  relation: main_file
  success: 1
file_date_updated: 2024-01-10T13:39:42Z
has_accepted_license: '1'
intvolume: '        24'
isi: 1
issue: '22'
keyword:
- Inorganic Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Computer Science Applications
- Spectroscopy
- Molecular Biology
- General Medicine
- Catalysis
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: International Journal of Molecular Sciences
publication_identifier:
  issn:
  - 1422-0067
publication_status: published
publisher: MDPI
quality_controlled: '1'
status: public
title: Phytaspase Is capable of detaching the endoplasmic reticulum retrieval signal
  from tobacco calreticulin-3
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 24
year: '2023'
...
---
_id: '11489'
abstract:
- lang: eng
  text: Much of plant development depends on cell-to-cell redistribution of the plant
    hormone auxin, which is facilitated by the plasma membrane (PM) localized PIN
    FORMED (PIN) proteins. Auxin export activity, developmental roles, subcellular
    trafficking, and polarity of PINs have been well studied, but their structure
    remains elusive besides a rough outline that they contain two groups of 5 alpha-helices
    connected by a large hydrophilic loop (HL). Here, we focus on the PIN1 HL as we
    could produce it in sufficient quantities for biochemical investigations to provide
    insights into its secondary structure. Circular dichroism (CD) studies revealed
    its nature as an intrinsically disordered protein (IDP), manifested by the increase
    of structure content upon thermal melting. Consistent with IDPs serving as interaction
    platforms, PIN1 loops homodimerize. PIN1 HL cytoplasmic overexpression in Arabidopsis
    disrupts early endocytic trafficking of PIN1 and PIN2 and causes defects in the
    cotyledon vasculature formation. In summary, we demonstrate that PIN1 HL has an
    intrinsically disordered nature, which must be considered to gain further structural
    insights. Some secondary structures may form transiently during pairing with known
    and yet-to-be-discovered interactors.
acknowledgement: 'We thank Charo del Genio from Coventry University and Richard Napier
  from the University of Warwick for helpful discussion concerning protein modeling
  and inspiration concerning CD spectroscopy, respectively. We thank Jan Hejatko for
  sharing the published AHP2 construct. We also thank Josef Houser from the core facility
  BIC CEITEC for valuable assistance, discussions, and ideas relating to CD. We acknowledge
  the: Core Facility CELLIM of CEITEC supported by the Czech-BioImaging large RI project
  (LM2018129 funded by MEYS CR), part of the Euro-BioImaging (www.eurobioimaging.eu
  accessed on 1 January 2016) ALM and medical imaging Node (Brno, CZ), CF Biomolecular
  Interactions and Crystallization of CIISB, Instruct-CZ Centre, supported by MEYS
  CR (LM2018127) and European Regional Development Fund-Project “UP CIISB“ (No. CZ.02.1.01/0.0/0.0/18_046/0015974)
  for their support with obtaining scientific data presented in this paper; Plant
  Sciences Core Facility of CEITEC Masaryk University for technical support. Open
  Access Funding by the Austrian Science Fund (FWF).'
article_processing_charge: Yes
article_type: original
author:
- first_name: V
  full_name: Bilanovičová, V
  last_name: Bilanovičová
- first_name: N
  full_name: Rýdza, N
  last_name: Rýdza
- first_name: L
  full_name: Koczka, L
  last_name: Koczka
- first_name: M
  full_name: Hess, M
  last_name: Hess
- first_name: E
  full_name: Feraru, E
  last_name: Feraru
- first_name: Jiří
  full_name: Friml, Jiří
  id: 4159519E-F248-11E8-B48F-1D18A9856A87
  last_name: Friml
  orcid: 0000-0002-8302-7596
- first_name: T
  full_name: Nodzyński, T
  last_name: Nodzyński
citation:
  ama: Bilanovičová V, Rýdza N, Koczka L, et al. The hydrophilic loop of Arabidopsis
    PIN1 auxin efflux carrier harbors hallmarks of an intrinsically disordered protein.
    <i>International Journal of Molecular Sciences</i>. 2022;23(11):6352. doi:<a href="https://doi.org/10.3390/ijms23116352">10.3390/ijms23116352</a>
  apa: Bilanovičová, V., Rýdza, N., Koczka, L., Hess, M., Feraru, E., Friml, J., &#38;
    Nodzyński, T. (2022). The hydrophilic loop of Arabidopsis PIN1 auxin efflux carrier
    harbors hallmarks of an intrinsically disordered protein. <i>International Journal
    of Molecular Sciences</i>. MDPI. <a href="https://doi.org/10.3390/ijms23116352">https://doi.org/10.3390/ijms23116352</a>
  chicago: Bilanovičová, V, N Rýdza, L Koczka, M Hess, E Feraru, Jiří Friml, and T
    Nodzyński. “The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux Carrier Harbors
    Hallmarks of an Intrinsically Disordered Protein.” <i>International Journal of
    Molecular Sciences</i>. MDPI, 2022. <a href="https://doi.org/10.3390/ijms23116352">https://doi.org/10.3390/ijms23116352</a>.
  ieee: V. Bilanovičová <i>et al.</i>, “The hydrophilic loop of Arabidopsis PIN1 auxin
    efflux carrier harbors hallmarks of an intrinsically disordered protein,” <i>International
    Journal of Molecular Sciences</i>, vol. 23, no. 11. MDPI, p. 6352, 2022.
  ista: Bilanovičová V, Rýdza N, Koczka L, Hess M, Feraru E, Friml J, Nodzyński T.
    2022. The hydrophilic loop of Arabidopsis PIN1 auxin efflux carrier harbors hallmarks
    of an intrinsically disordered protein. International Journal of Molecular Sciences.
    23(11), 6352.
  mla: Bilanovičová, V., et al. “The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux
    Carrier Harbors Hallmarks of an Intrinsically Disordered Protein.” <i>International
    Journal of Molecular Sciences</i>, vol. 23, no. 11, MDPI, 2022, p. 6352, doi:<a
    href="https://doi.org/10.3390/ijms23116352">10.3390/ijms23116352</a>.
  short: V. Bilanovičová, N. Rýdza, L. Koczka, M. Hess, E. Feraru, J. Friml, T. Nodzyński,
    International Journal of Molecular Sciences 23 (2022) 6352.
date_created: 2022-07-05T15:14:34Z
date_published: 2022-06-06T00:00:00Z
date_updated: 2023-08-09T10:13:57Z
day: '06'
ddc:
- '570'
department:
- _id: JiFr
doi: 10.3390/ijms23116352
external_id:
  isi:
  - '000808733300001'
  pmid:
  - '35683031'
file:
- access_level: open_access
  checksum: e997a57a928ec9d51fad8ce824a05935
  content_type: application/pdf
  creator: cchlebak
  date_created: 2022-07-06T07:36:59Z
  date_updated: 2022-07-06T07:36:59Z
  file_id: '11492'
  file_name: 2022_IntJMolSci_Bilanovicova.pdf
  file_size: 2324542
  relation: main_file
  success: 1
file_date_updated: 2022-07-06T07:36:59Z
has_accepted_license: '1'
intvolume: '        23'
isi: 1
issue: '11'
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
page: '6352'
pmid: 1
project:
- _id: 262EF96E-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: P29988
  name: RNA-directed DNA methylation in plant development
publication: International Journal of Molecular Sciences
publication_identifier:
  issn:
  - 1422-0067
publication_status: published
publisher: MDPI
quality_controlled: '1'
status: public
title: The hydrophilic loop of Arabidopsis PIN1 auxin efflux carrier harbors hallmarks
  of an intrinsically disordered protein
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2022'
...
---
_id: '8225'
abstract:
- lang: eng
  text: Birch pollen allergy is among the most prevalent pollen allergies in Northern
    and Central Europe. This IgE-mediated disease can be treated with allergen immunotherapy
    (AIT), which typically gives rise to IgG antibodies inducing tolerance. Although
    the main mechanisms of allergen immunotherapy (AIT) are known, questions regarding
    possible Fc-mediated effects of IgG antibodies remain unanswered. This can mainly
    be attributed to the unavailability of appropriate tools, i.e., well-characterised
    recombinant antibodies (rAbs). We hereby aimed at providing human rAbs of several
    classes for mechanistic studies and as possible candidates for passive immunotherapy.
    We engineered IgE, IgG1, and IgG4 sharing the same variable region against the
    major birch pollen allergen Bet v 1 using Polymerase Incomplete Primer Extension
    (PIPE) cloning. We tested IgE functionality and IgG blocking capabilities using
    appropriate model cell lines. In vitro studies showed IgE engagement with FcεRI
    and CD23 and Bet v 1-dependent degranulation. Overall, we hereby present fully
    functional, human IgE, IgG1, and IgG4 sharing the same variable region against
    Bet v 1 and showcase possible applications in first mechanistic studies. Furthermore,
    our IgG antibodies might be useful candidates for passive immunotherapy of birch
    pollen allergy.
article_number: '5693'
article_processing_charge: No
article_type: original
author:
- first_name: Verena K.
  full_name: Köhler, Verena K.
  last_name: Köhler
  orcid: 0000-0001-5581-398X
- first_name: Silvia
  full_name: Crescioli, Silvia
  last_name: Crescioli
  orcid: 0000-0002-1909-5957
- first_name: Judit
  full_name: Fazekas-Singer, Judit
  id: 36432834-F248-11E8-B48F-1D18A9856A87
  last_name: Fazekas-Singer
  orcid: 0000-0002-8777-3502
- first_name: Heather J.
  full_name: Bax, Heather J.
  last_name: Bax
  orcid: 0000-0003-0432-4160
- first_name: Gerhard
  full_name: Hofer, Gerhard
  last_name: Hofer
- first_name: Christina L.
  full_name: Pranger, Christina L.
  last_name: Pranger
- first_name: Karin
  full_name: Hufnagl, Karin
  last_name: Hufnagl
- first_name: Rodolfo
  full_name: Bianchini, Rodolfo
  last_name: Bianchini
  orcid: 0000-0003-0351-6937
- first_name: Sabine
  full_name: Flicker, Sabine
  last_name: Flicker
  orcid: 0000-0003-4768-8693
- first_name: Walter
  full_name: Keller, Walter
  last_name: Keller
  orcid: 0000-0002-2261-958X
- first_name: Sophia N.
  full_name: Karagiannis, Sophia N.
  last_name: Karagiannis
  orcid: 0000-0002-4100-7810
- first_name: Erika
  full_name: Jensen-Jarolim, Erika
  last_name: Jensen-Jarolim
  orcid: 0000-0003-4019-5765
citation:
  ama: 'Köhler VK, Crescioli S, Singer J, et al. Filling the antibody pipeline in
    allergy: PIPE cloning of IgE, IgG1 and IgG4 against the major birch pollen allergen
    Bet v 1. <i>International Journal of Molecular Sciences</i>. 2020;21(16). doi:<a
    href="https://doi.org/10.3390/ijms21165693">10.3390/ijms21165693</a>'
  apa: 'Köhler, V. K., Crescioli, S., Singer, J., Bax, H. J., Hofer, G., Pranger,
    C. L., … Jensen-Jarolim, E. (2020). Filling the antibody pipeline in allergy:
    PIPE cloning of IgE, IgG1 and IgG4 against the major birch pollen allergen Bet
    v 1. <i>International Journal of Molecular Sciences</i>. MDPI. <a href="https://doi.org/10.3390/ijms21165693">https://doi.org/10.3390/ijms21165693</a>'
  chicago: 'Köhler, Verena K., Silvia Crescioli, Judit Singer, Heather J. Bax, Gerhard
    Hofer, Christina L. Pranger, Karin Hufnagl, et al. “Filling the Antibody Pipeline
    in Allergy: PIPE Cloning of IgE, IgG1 and IgG4 against the Major Birch Pollen
    Allergen Bet v 1.” <i>International Journal of Molecular Sciences</i>. MDPI, 2020.
    <a href="https://doi.org/10.3390/ijms21165693">https://doi.org/10.3390/ijms21165693</a>.'
  ieee: 'V. K. Köhler <i>et al.</i>, “Filling the antibody pipeline in allergy: PIPE
    cloning of IgE, IgG1 and IgG4 against the major birch pollen allergen Bet v 1,”
    <i>International Journal of Molecular Sciences</i>, vol. 21, no. 16. MDPI, 2020.'
  ista: 'Köhler VK, Crescioli S, Singer J, Bax HJ, Hofer G, Pranger CL, Hufnagl K,
    Bianchini R, Flicker S, Keller W, Karagiannis SN, Jensen-Jarolim E. 2020. Filling
    the antibody pipeline in allergy: PIPE cloning of IgE, IgG1 and IgG4 against the
    major birch pollen allergen Bet v 1. International Journal of Molecular Sciences.
    21(16), 5693.'
  mla: 'Köhler, Verena K., et al. “Filling the Antibody Pipeline in Allergy: PIPE
    Cloning of IgE, IgG1 and IgG4 against the Major Birch Pollen Allergen Bet v 1.”
    <i>International Journal of Molecular Sciences</i>, vol. 21, no. 16, 5693, MDPI,
    2020, doi:<a href="https://doi.org/10.3390/ijms21165693">10.3390/ijms21165693</a>.'
  short: V.K. Köhler, S. Crescioli, J. Singer, H.J. Bax, G. Hofer, C.L. Pranger, K.
    Hufnagl, R. Bianchini, S. Flicker, W. Keller, S.N. Karagiannis, E. Jensen-Jarolim,
    International Journal of Molecular Sciences 21 (2020).
date_created: 2020-08-10T11:47:29Z
date_published: 2020-08-08T00:00:00Z
date_updated: 2021-01-12T08:17:34Z
day: '08'
ddc:
- '570'
doi: 10.3390/ijms21165693
extern: '1'
external_id:
  pmid:
  - '32784509'
file:
- access_level: open_access
  checksum: dac7ccef7cdcea9be292664d8c488425
  content_type: application/pdf
  creator: dernst
  date_created: 2020-09-10T07:06:22Z
  date_updated: 2020-09-10T07:06:22Z
  file_id: '8356'
  file_name: 2020_IntMolecSciences_Koehler.pdf
  file_size: 2680908
  relation: main_file
  success: 1
file_date_updated: 2020-09-10T07:06:22Z
has_accepted_license: '1'
intvolume: '        21'
issue: '16'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: International Journal of Molecular Sciences
publication_identifier:
  issn:
  - 1422-0067
publication_status: published
publisher: MDPI
quality_controlled: '1'
status: public
title: 'Filling the antibody pipeline in allergy: PIPE cloning of IgE, IgG1 and IgG4
  against the major birch pollen allergen Bet v 1'
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 21
year: '2020'
...