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  1. Article ; Online: Salvage Procedures for Facial Reanimation With Neurovascular Flaps When Previous Surgeries Failed: Is Homolateral Vessel or Nerve Depletion a Contraindication?

    Ibarra, Gorka / Lasso, Jose M

    Annals of plastic surgery

    2022  Volume 89, Issue 2, Page(s) 196–200

    Abstract: Background: Facial paralysis reconstruction can be difficult in extensive defects after complex facial or cranial base tumor resection and radiotherapy or when primary smile reanimation attempt has failed. The surgical challenge is more complicated when ...

    Abstract Background: Facial paralysis reconstruction can be difficult in extensive defects after complex facial or cranial base tumor resection and radiotherapy or when primary smile reanimation attempt has failed. The surgical challenge is more complicated when defects are associated with recipient vessels or nerves depletion. This scenario has not been well described in the literature, and the present article will address the alternatives that plastic surgeons may use in these circumstances.
    Methods: Seventy-five patients operated in the Hospital Gregorio Marañon between 2008 and 2020, for dynamic reconstruction of facial paralysis, were retrospectively evaluated, collecting data about previous facial nerve surgeries, radiotherapy, chemotherapy, recipient nerve for motor restoration and vessels used for free flaps, type of neurovascular free flap (NVFF), and functional score before and after the facial reanimation surgery. Patients presenting recipient vessel and/or nerve depletion after several facial surgeries requiring a variation from the common NVFF surgical protocol were included in this study.
    Results: Six cases (8%) with facial paralysis and absent recipient homolateral vessels or nerves after severe cranial base surgery, parotid malignancies, or schwannoma surgery were included. Two patients had an immediate functional reconstruction during the oncologic resection surgery, and 4 patients had a delayed reconstruction. Three patients had previous reconstruction with free flaps, and the vascular pedicles of previous flaps were used for the new NVFF. In the other 3 cases, interposition vein grafts to the contralateral recipient vessels were required to perform NVFF. Masseteric nerve in 4 cases, hypoglossal nerve and posterior branch of the deep temporal nerve in 1 case each, were used as recipient nerves. House-Brackmann score improved in all patients after surgery.
    Conclusions: Neurovascular free flap can be successfully performed to restore facial motion after depletion of homolateral recipient vessels or nerves after previous facial or cranial base surgeries. In these cases, interposition vascular grafts or the pedicle of previous flaps are essential to provide vascularization as well as an optimal orientation of flaps, to reach recipient nerves in a 1-step procedure.
    MeSH term(s) Contraindications ; Facial Nerve/surgery ; Facial Paralysis/surgery ; Free Tissue Flaps/transplantation ; Humans ; Reconstructive Surgical Procedures/methods ; Retrospective Studies
    Language English
    Publishing date 2022-01-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 423835-7
    ISSN 1536-3708 ; 0148-7043
    ISSN (online) 1536-3708
    ISSN 0148-7043
    DOI 10.1097/SAP.0000000000003061
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Editorial: Influence of Protein-Protein Interactions (PPIs) on the Outcome of Viral Infections.

    Jangra, Rohit K / Llabrés, Mercè / Guardado-Calvo, Pablo / Mittler, Eva / Lasso, Gorka

    Frontiers in microbiology

    2022  Volume 13, Page(s) 943379

    Language English
    Publishing date 2022-06-27
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2022.943379
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: A Sweep of Earth's Virome Reveals Host-Guided Viral Protein Structural Mimicry and Points to Determinants of Human Disease.

    Lasso, Gorka / Honig, Barry / Shapira, Sagi D

    Cell systems

    2020  Volume 12, Issue 1, Page(s) 82–91.e3

    Abstract: Viruses deploy genetically encoded strategies to coopt host machinery and support viral replicative cycles. Here, we use protein structure similarity to scan for molecular mimicry, manifested by structural similarity between viral and endogenous host ... ...

    Abstract Viruses deploy genetically encoded strategies to coopt host machinery and support viral replicative cycles. Here, we use protein structure similarity to scan for molecular mimicry, manifested by structural similarity between viral and endogenous host proteins, across thousands of cataloged viruses and hosts spanning broad ecological niches and taxonomic range, including bacteria, plants and fungi, invertebrates, and vertebrates. This survey identified over 6,000,000 instances of structural mimicry; more than 70% of viral mimics cannot be discerned through protein sequence alone. We demonstrate that the manner and degree to which viruses exploit molecular mimicry varies by genome size and nucleic acid type and identify 158 human proteins that are mimicked by coronaviruses, providing clues about cellular processes driving pathogenesis. Our observations point to molecular mimicry as a pervasive strategy employed by viruses and indicate that the protein structure space used by a given virus is dictated by the host proteome. A record of this paper's transparent peer review process is included in the Supplemental Information.
    MeSH term(s) Animals ; Coronavirus/chemistry ; Coronavirus/genetics ; Culicidae ; Databases, Genetic ; Host-Pathogen Interactions/genetics ; Humans ; Molecular Mimicry/genetics ; Protein Structure, Secondary ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Virome/genetics ; Virus Diseases/epidemiology ; Virus Diseases/genetics ; Viruses/chemistry ; Viruses/genetics
    Chemical Substances Viral Proteins
    Keywords covid19
    Language English
    Publishing date 2020-10-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2854138-8
    ISSN 2405-4720 ; 2405-4712
    ISSN (online) 2405-4720
    ISSN 2405-4712
    DOI 10.1016/j.cels.2020.09.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: A Sweep of Earth's Virome Reveals Host-Guided Viral Protein Structural Mimicry and Points to Determinants of Human Disease

    Lasso, Gorka / Honig, Barry / Shapira, Sagi D

    Cell Syst

    Abstract: Viruses deploy genetically encoded strategies to coopt host machinery and support viral replicative cycles. Here, we use protein structure similarity to scan for molecular mimicry, manifested by structural similarity between viral and endogenous host ... ...

    Abstract Viruses deploy genetically encoded strategies to coopt host machinery and support viral replicative cycles. Here, we use protein structure similarity to scan for molecular mimicry, manifested by structural similarity between viral and endogenous host proteins, across thousands of cataloged viruses and hosts spanning broad ecological niches and taxonomic range, including bacteria, plants and fungi, invertebrates, and vertebrates. This survey identified over 6,000,000 instances of structural mimicry; more than 70% of viral mimics cannot be discerned through protein sequence alone. We demonstrate that the manner and degree to which viruses exploit molecular mimicry varies by genome size and nucleic acid type and identify 158 human proteins that are mimicked by coronaviruses, providing clues about cellular processes driving pathogenesis. Our observations point to molecular mimicry as a pervasive strategy employed by viruses and indicate that the protein structure space used by a given virus is dictated by the host proteome. A record of this paper's transparent peer review process is included in the Supplemental Information.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #856528
    Database COVID19

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  5. Article ; Online: A sweep of earth’s virome reveals host-guided viral protein structural mimicry; with implications for human disease

    Lasso, Gorka / Honig, Barry / Shapira, Sagi D.

    bioRxiv

    Abstract: Viruses deploy an array of genetically encoded strategies to coopt host machinery and support viral replicative cycles. Molecular mimicry, manifested by structural similarity between viral and endogenous host proteins, allow viruses to harness or disrupt ...

    Abstract Viruses deploy an array of genetically encoded strategies to coopt host machinery and support viral replicative cycles. Molecular mimicry, manifested by structural similarity between viral and endogenous host proteins, allow viruses to harness or disrupt cellular functions including nucleic acid metabolism and modulation of immune responses. Here, we use protein structure similarity to scan for virally encoded structure mimics across thousands of catalogued viruses and hosts spanning broad ecological niches and taxonomic range, including bacteria, plants and fungi, invertebrates and vertebrates. Our survey identified over 6,000,000 instances of structural mimicry, the vast majority of which (>70%) cannot be discerned through protein sequence. The results point to molecular mimicry as a pervasive strategy employed by viruses and indicate that the protein structure space used by a given virus is dictated by the host proteome. Interrogation of proteins mimicked by human-infecting viruses points to broad diversification of cellular pathways targeted via structural mimicry, identifies biological processes that may underly autoimmune disorders, and reveals virally encoded mimics that may be leveraged to engineer synthetic metabolic circuits or may serve as targets for therapeutics. Moreover, the manner and degree to which viruses exploit molecular mimicry varies by genome size and nucleic acid type, with ssRNA viruses circumventing limitations of their small genomes by mimicking human proteins to a greater extent than their large dsDNA counterparts. Finally, we identified over 140 cellular proteins that are mimicked by CoV, providing clues about cellular processes driving the pathogenesis of the ongoing COVID-19 pandemic.
    Keywords covid19
    Publisher BioRxiv
    Document type Article ; Online
    DOI 10.1101/2020.06.18.159467
    Database COVID19

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  6. Article ; Online: Anatomic and histomorphometric study of the nerve to the vastus lateralis in cadaver for its clinical application in facial reanimation.

    Lasso, Jose M / Ibarra, Gorka / Rivera, Andres / Fernandez-Ibarburu, Borja / Olivares, Martin / de la Cruz, Ignacio / Gomez-Navarro, Yesica / Garcia, Maria

    Microsurgery

    2023  Volume 43, Issue 4, Page(s) 365–372

    Abstract: Background: The innervated vastus lateralis flap (IVLF) is a barely used possibility for facial palsy reconstruction because of its thickness compared to the gracilis, latissimus dorsi, and pectoralis minor flaps. The aim of this study is to perform a ... ...

    Abstract Background: The innervated vastus lateralis flap (IVLF) is a barely used possibility for facial palsy reconstruction because of its thickness compared to the gracilis, latissimus dorsi, and pectoralis minor flaps. The aim of this study is to perform a precise description of the intramuscular distribution of the nerve motor branches and its relationship with the vascular pedicle in order to harvest a segmental muscle flap with the best contractile strength to restore facial reanimation.
    Methods: The study was performed on 16 adult cadaver thighs identifying the vastus lateralis muscle and the distribution and relationships of its neurovascular pedicle and branches. We evaluated where the nerve pierced the muscle and the course of the nerve within it. Transverse segments of the nerve were obtained from the proximal and distal ends of the nerve and stained using anti-ChAT (Choline acetyltransferase) antibodies which are specific of motor neurons.
    Results: A nerve for the vastus lateralis from the posterior division of the femoral nerve divided into 2 branches in 56% of cases; the principal branch coursed along the vascular pedicle and pierced the muscle more proximally than the respective vessels, and a minor branch that pierced the muscle 25-60 mm proximally. There were 3 main intramuscular branches. The nerve length (mean 132.65 ± 22.89 mm) allowed to reach the contralateral side of the face in almost all cases (95%). The mean ChAT positive fibers was 351.0 ± 92.4/mm
    Conclusion: We propose the IVLF as a one-step surgical flap for facial paralysis reanimation due to the constant neurovascular pattern and lengthy pedicle. The amount of motor fibers in several segments of the nerve is appropriate to produce a powerful contraction for dynamic reconstruction.
    MeSH term(s) Adult ; Humans ; Quadriceps Muscle/innervation ; Surgical Flaps/blood supply ; Facial Paralysis/surgery ; Facial Paralysis/etiology ; Femoral Nerve ; Cadaver ; Facial Nerve/surgery
    Language English
    Publishing date 2023-01-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 605524-2
    ISSN 1098-2752 ; 0738-1085
    ISSN (online) 1098-2752
    ISSN 0738-1085
    DOI 10.1002/micr.31005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Author Correction: Two point mutations in protocadherin-1 disrupt hantavirus recognition and afford protection against lethal infection.

    Slough, Megan M / Li, Rong / Herbert, Andrew S / Lasso, Gorka / Kuehne, Ana I / Monticelli, Stephanie R / Bakken, Russell R / Liu, Yanan / Ghosh, Agnidipta / Moreau, Alicia M / Zeng, Xiankun / Rey, Félix A / Guardado-Calvo, Pablo / Almo, Steven C / Dye, John M / Jangra, Rohit K / Wang, Zhongde / Chandran, Kartik

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 5924

    Language English
    Publishing date 2023-09-22
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-41659-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Efficacy of Povidone Iodine Against Microbial Biofilms in Breast Implants With Different Textures: Results From an

    Fernández-Ibarburu, Borja / Díaz-Navarro, Marta / Ibarra, Gorka / Rivera, Andrés / Hafian, Rama / Irigoyen, Ãlvaro / Carrillo, Raquel / Pérez-Cano, Rosa / Muñoz, Patricia / García-Ruano, Ángela / Lasso, José M / Guembe, María

    Frontiers in microbiology

    2022  Volume 13, Page(s) 868347

    Abstract: Background: In the practice of breast augmentation and reconstruction, implant irrigation with various solutions has been widely used to prevent infection and capsular contracture, but to date, there is no consensus on the optimal protocol to use. ... ...

    Abstract Background: In the practice of breast augmentation and reconstruction, implant irrigation with various solutions has been widely used to prevent infection and capsular contracture, but to date, there is no consensus on the optimal protocol to use. Recently, application of povidone iodine (PI) for 30 min has shown
    Methods: We tested the efficacy of 10% PI at 1', 3', and 5' against biofilms of 8 strains (2 ATCC and 6 clinical) of
    Results: All textured implants treated with PI at any of the 3 exposure times reduced 100% bacterial load by culture. However, none of the implants reached enough clinical significance in percentage reduction of living cells. Regarding bacterial density, only 25-50 μm Polytxt
    Conclusion: PI is able to inhibit bacterial growth applied on the surface of breast implants regardless of the exposure time. However, no significant reduction on living cells or bacterial density was observed. This lack of correlation may be caused by differences in texture that directly affect PI absorption.
    Language English
    Publishing date 2022-03-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2022.868347
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Two point mutations in protocadherin-1 disrupt hantavirus recognition and afford protection against lethal infection.

    Slough, Megan M / Li, Rong / Herbert, Andrew S / Lasso, Gorka / Kuehne, Ana I / Monticelli, Stephanie R / Bakken, Russell R / Liu, Yanan / Ghosh, Agnidipta / Moreau, Alicia M / Zeng, Xiankun / Rey, Félix A / Guardado-Calvo, Pablo / Almo, Steven C / Dye, John M / Jangra, Rohit K / Wang, Zhongde / Chandran, Kartik

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 4454

    Abstract: Andes virus (ANDV) and Sin Nombre virus (SNV) are the etiologic agents of severe hantavirus cardiopulmonary syndrome (HCPS) in the Americas for which no FDA-approved countermeasures are available. Protocadherin-1 (PCDH1), a cadherin-superfamily protein ... ...

    Abstract Andes virus (ANDV) and Sin Nombre virus (SNV) are the etiologic agents of severe hantavirus cardiopulmonary syndrome (HCPS) in the Americas for which no FDA-approved countermeasures are available. Protocadherin-1 (PCDH1), a cadherin-superfamily protein recently identified as a critical host factor for ANDV and SNV, represents a new antiviral target; however, its precise role remains to be elucidated. Here, we use computational and experimental approaches to delineate the binding surface of the hantavirus glycoprotein complex on PCDH1's first extracellular cadherin repeat domain. Strikingly, a single amino acid residue in this PCDH1 surface influences the host species-specificity of SNV glycoprotein-PCDH1 interaction and cell entry. Mutation of this and a neighboring residue substantially protects Syrian hamsters from pulmonary disease and death caused by ANDV. We conclude that PCDH1 is a bona fide entry receptor for ANDV and SNV whose direct interaction with hantavirus glycoproteins could be targeted to develop new interventions against HCPS.
    MeSH term(s) Animals ; Cricetinae ; Orthohantavirus ; Point Mutation ; Protocadherins ; Communicable Diseases ; Cadherins ; Mesocricetus ; RNA Viruses ; Syndrome
    Chemical Substances Protocadherins ; Cadherins
    Language English
    Publishing date 2023-07-24
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-40126-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Two point mutations in protocadherin-1 disrupt hantavirus recognition and afford protection against lethal infection

    Megan M. Slough / Rong Li / Andrew S. Herbert / Gorka Lasso / Ana I. Kuehne / Stephanie R. Monticelli / Russell R. Bakken / Yanan Liu / Agnidipta Ghosh / Alicia M. Moreau / Xiankun Zeng / Félix A. Rey / Pablo Guardado-Calvo / Steven C. Almo / John M. Dye / Rohit K. Jangra / Zhongde Wang / Kartik Chandran

    Nature Communications, Vol 14, Iss 1, Pp 1-

    2023  Volume 17

    Abstract: Abstract Andes virus (ANDV) and Sin Nombre virus (SNV) are the etiologic agents of severe hantavirus cardiopulmonary syndrome (HCPS) in the Americas for which no FDA-approved countermeasures are available. Protocadherin-1 (PCDH1), a cadherin-superfamily ... ...

    Abstract Abstract Andes virus (ANDV) and Sin Nombre virus (SNV) are the etiologic agents of severe hantavirus cardiopulmonary syndrome (HCPS) in the Americas for which no FDA-approved countermeasures are available. Protocadherin-1 (PCDH1), a cadherin-superfamily protein recently identified as a critical host factor for ANDV and SNV, represents a new antiviral target; however, its precise role remains to be elucidated. Here, we use computational and experimental approaches to delineate the binding surface of the hantavirus glycoprotein complex on PCDH1’s first extracellular cadherin repeat domain. Strikingly, a single amino acid residue in this PCDH1 surface influences the host species-specificity of SNV glycoprotein-PCDH1 interaction and cell entry. Mutation of this and a neighboring residue substantially protects Syrian hamsters from pulmonary disease and death caused by ANDV. We conclude that PCDH1 is a bona fide entry receptor for ANDV and SNV whose direct interaction with hantavirus glycoproteins could be targeted to develop new interventions against HCPS.
    Keywords Science ; Q
    Subject code 570
    Language English
    Publishing date 2023-07-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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