Patents by Inventor Lorena Rodriguez Rubio

Lorena Rodriguez Rubio has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).

  • Patent number: 9868943
    Abstract: Virion-associated peptidoglycan hydrolases have a potential as antimicrobial agents due to their ability to lyse Gram positive bacteria on contact. Fusion proteins HydH5SH3b and HydH5Lyso comprising full-length peptidoglycan hydrolase HydH5 from the Staphylococcus aureus bacteriophage vB_SauS-phi-IPLA88 in combination with the SH3b cell wall-binding domain from lysostaphin or full length lysostaphin, respectively, exhibited high lytic activity against live S. aureus cells. CHAPSH3b, a HydH5 CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) domain from truncated HydH5 in combination with the SH3b domain of lysostaphin, exhibited the highest lytic activity against live S. aureus cells. HydH5 and its derivative fusions lysed bovine and human S. aureus, methicillin-resistant S. aureus (MRSA) N315 strain, and human S. epidermidis strains in zymogram, plate lysis and turbidity reduction assays.
    Type: Grant
    Filed: February 12, 2015
    Date of Patent: January 16, 2018
    Assignee: The United States of America, as represented by The Secretary of Agriculture
    Inventors: David M. Donovan, Lorena Rodriguez Rubio, Beatriz Martinez Fernandez, Ana Rodriguez, Pilar Garcia Suarez
  • Publication number: 20150247138
    Abstract: Virion-associated peptidoglycan hydrolases have a potential as antimicrobial agents due to their ability to lyse Gram positive bacteria on contact. Full-length HydH5, a virion-associated peptidoglycan hydrolase from the Staphylococcus aureus bacteriophage vB_SauS-phi-IPLA88, and two truncated derivatives, containing only the CHAP domain, exhibited high lytic activity against live S. aureus cells. Three different fusion proteins were created and showed higher staphylolytic activity than the parental enzyme or its deletion construct. Parental and fusion proteins lysed S. aureus cells in zymograms, plate lysis and turbidity reduction assays. In plate lysis assays, HydH5 and its derivative fusions lysed bovine and human S. aureus, S. aureus MRSA N315 strain, and human Staphylococcus epidermidis strains.
    Type: Application
    Filed: February 12, 2015
    Publication date: September 3, 2015
    Inventors: David M. Donovan, Lorena Rodriguez Rubio, Beatriz Martinez Fernandez, Ana Rodriguez, Pilar Garcia Suarez
  • Patent number: 8986695
    Abstract: Virion-associated peptidoglycan hydrolases have a potential as antimicrobial agents due to their ability to lyse Gram positive bacteria on contact. Full-length HydH5, a virion-associated peptidoglycan hydrolase from the Staphylococcus aureus bacteriophage vB_SauS-phi-IPLA88, and two truncated derivatives, containing only the CHAP domain, exhibited high lytic activity against live S. aureus cells. Three different fusion proteins were created and showed higher staphylolytic activity than the parental enzyme or its deletion construct. Parental and fusion proteins lysed S. aureus cells in zymograms, plate lysis and turbidity reduction assays. In plate lysis assays, HydH5 and its derivative fusions lysed bovine and human S. aureus, S. aureus MRSA N315 strain, and human Staphylococcus epidermidis strains.
    Type: Grant
    Filed: November 17, 2011
    Date of Patent: March 24, 2015
    Assignee: The United States of America, as represented by The Secretary of Agriculture
    Inventors: David M. Donovan, Lorena Rodriguez Rubio, Beatriz Martinez Fernandez, Ana Rodriguez, Pilar Garcia Suarez
  • Publication number: 20130129697
    Abstract: Virion-associated peptidoglycan hydrolases have a potential as antimicrobial agents due to their ability to lyse Gram positive bacteria on contact. Full-length HydH5, a virion-associated peptidoglycan hydrolase from the Staphylococcus aureus bacteriophage vB_SauS-phi-IPLA88, and two truncated derivatives, containing only the CHAP domain, exhibited high lytic activity against live S. aureus cells. Three different fusion proteins were created and showed higher staphylolytic activity than the parental enzyme or its deletion construct. Parental and, fusion proteins lysed S. aureus cells in zymograms, plate lysis and turbidity reduction assays. In plate lysis assays, HydH5 and its derivative fusions lysed bovine and human S. aureus, S. aureus MRSA N315 strain, and human Staphylococcus epidermidis strains.
    Type: Application
    Filed: November 17, 2011
    Publication date: May 23, 2013
    Inventors: David M. Donovan, Lorena Rodriguez Rubio, Beatriz Martinez Fernandez, Ana Rodriguez, Pilar Garcia Suarez