The Experts below are selected from a list of 81 Experts worldwide ranked by ideXlab platform
Yong Gao - One of the best experts on this subject based on the ideXlab platform.
-
Functional bottlenecks for generation of HIV-1 intersubtype Env recombinants
Retrovirology, 2015Co-Authors: Bernard S. Bagaya, José F. Vega, Meijuan Tian, Gabrielle C. Nickel, Kendall C. Krebs, Eric J. Arts, Yong GaoAbstract:Background Intersubtype recombination is a powerful driving force for HIV evolution, impacting both HIV-1 diversity within an infected individual and within the global epidemic. This study examines if Viral Protein function/fitness is the major constraint shaping selection of recombination hotspots in replication-competent HIV-1 progeny. A better understanding of the interplay between Viral Protein Structure-function and recombination may provide insights into both vaccine design and drug development. Results In vitro HIV-1 dual infections were used to recombine subtypes A and D isolates and examine breakpoints in the Env glycoProteins. The entire env genes of 21 A/D recombinants with breakpoints in gp120 were non-functional when cloned into the laboratory strain, NL4-3. Likewise, cloning of A/D gp120 coding regions also produced dead viruses with non-functional Envs. 4/9 replication-competent viruses with functional Env’s were obtained when just the V1-V5 regions of these same A/D recombinants (i.e. same A/D breakpoints as above) were cloned into NL4-3. Conclusion These findings on functional A/D Env recombinants combined with structural models of Env suggest a conserved interplay between the C1 domain with C5 domain of gp120 and extracellular domain of gp41. Models also reveal a co-evolution within C1, C5, and ecto-gp41 domains which might explain the paucity of intersubtype recombination in the gp120 V1-V5 regions, despite their hypervariability. At least HIV-1 A/D intersubtype recombination in gp120 may result in a C1 from one subtype incompatible with a C5/gp41 from another subtype.
-
Functional bottlenecks for generation of HIV-1 intersubtype Env recombinants
Retrovirology, 2015Co-Authors: Bernard S. Bagaya, José F. Vega, Meijuan Tian, Kendall C. Krebs, Eric J. Arts, Gabrielle Nickel, Yong GaoAbstract:Intersubtype recombination is a powerful driving force for HIV evolution, impacting both HIV-1 diversity within an infected individual and within the global epidemic. This study examines if Viral Protein function/fitness is the major constraint shaping selection of recombination hotspots in replication-competent HIV-1 progeny. A better understanding of the interplay between Viral Protein Structure-function and recombination may provide insights into both vaccine design and drug development. In vitro HIV-1 dual infections were used to recombine subtypes A and D isolates and examine breakpoints in the Env glycoProteins. The entire env genes of 21 A/D recombinants with breakpoints in gp120 were non-functional when cloned into the laboratory strain, NL4-3. Likewise, cloning of A/D gp120 coding regions also produced dead viruses with non-functional Envs. 4/9 replication-competent viruses with functional Env’s were obtained when just the V1-V5 regions of these same A/D recombinants (i.e. same A/D breakpoints as above) were cloned into NL4-3. These findings on functional A/D Env recombinants combined with structural models of Env suggest a conserved interplay between the C1 domain with C5 domain of gp120 and extracellular domain of gp41. Models also reveal a co-evolution within C1, C5, and ecto-gp41 domains which might explain the paucity of intersubtype recombination in the gp120 V1-V5 regions, despite their hypervariability. At least HIV-1 A/D intersubtype recombination in gp120 may result in a C1 from one subtype incompatible with a C5/gp41 from another subtype.
Sylvie German-retana - One of the best experts on this subject based on the ideXlab platform.
-
The Potyviridae Cylindrical Inclusion helicase: a key multipartner and multifunctional Protein
Molecular Plant-Microbe Interactions, 2014Co-Authors: Maud Sorel, Juan Antonio García, Sylvie German-retanaAbstract:A unique feature shared by all plant viruses of the Potyviridae family is the induction of characteristic pinwheel-shaped inclusion bodies in the cytoplasm of infected cells. These cylindrical inclusions are composed of the Viral encoded cylindrical inclusion helicase (CI Protein). Its helicase activity was characterized and its involvement in replication demonstrated through different reverse genetics approaches. Beside replication, the CI Protein is also involved in cell-to-cell and long distance movements, possibly through interactions with the recently discovered Viral P3N-PIPO Protein. Studies over the past two decades demonstrate that the CI Protein is present in several cellular compartments interacting with Viral and plant Protein partners likely involved in its various roles in different steps of Viral infection. Furthermore, the CI Protein acts as an avirulence factor in gene for gene interaction with dominant-resistance host genes, and a recessive-resistance overcoming factor. Although a significant amount of data concerning the potential functions and subcellular localization of this Protein has been published, no synthetic review is available on this important multifunctional Protein. In this review, we compile and integrate all information relevant to the current understanding of this Viral Protein Structure and function and present a mode of action for CI, combining replication and movement.
-
The Potyviridae cylindrical inclusion helicase: a key multipartner and multifunctional Protein.
Molecular plant-microbe interactions : MPMI, 2014Co-Authors: Maud Sorel, Juan Antonio García, Sylvie German-retanaAbstract:A unique feature shared by all plant viruses of the Potyviridae family is the induction of characteristic pinwheel-shaped inclusion bodies in the cytoplasm of infected cells. These cylindrical inclusions are composed of the Viral-encoded cylindrical inclusion helicase (CI Protein). Its helicase activity was characterized and its involvement in replication demonstrated through different reverse genetics approaches. In addition to replication, the CI Protein is also involved in cell-to-cell and long-distance movements, possibly through interactions with the recently discovered Viral P3N-PIPO Protein. Studies over the past two decades demonstrate that the CI Protein is present in several cellular compartments interacting with Viral and plant Protein partners likely involved in its various roles in different steps of Viral infection. Furthermore, the CI Protein acts as an avirulence factor in gene-for-gene interactions with dominant-resistance host genes and as a recessive-resistance overcoming factor. Although a significant amount of data concerning the potential functions and subcellular localization of this Protein has been published, no synthetic review is available on this important multifunctional Protein. In this review, we compile and integrate all information relevant to the current understanding of this Viral Protein Structure and function and present a mode of action for CI, combining replication and movement.
Bernard S. Bagaya - One of the best experts on this subject based on the ideXlab platform.
-
Functional bottlenecks for generation of HIV-1 intersubtype Env recombinants
Retrovirology, 2015Co-Authors: Bernard S. Bagaya, José F. Vega, Meijuan Tian, Gabrielle C. Nickel, Kendall C. Krebs, Eric J. Arts, Yong GaoAbstract:Background Intersubtype recombination is a powerful driving force for HIV evolution, impacting both HIV-1 diversity within an infected individual and within the global epidemic. This study examines if Viral Protein function/fitness is the major constraint shaping selection of recombination hotspots in replication-competent HIV-1 progeny. A better understanding of the interplay between Viral Protein Structure-function and recombination may provide insights into both vaccine design and drug development. Results In vitro HIV-1 dual infections were used to recombine subtypes A and D isolates and examine breakpoints in the Env glycoProteins. The entire env genes of 21 A/D recombinants with breakpoints in gp120 were non-functional when cloned into the laboratory strain, NL4-3. Likewise, cloning of A/D gp120 coding regions also produced dead viruses with non-functional Envs. 4/9 replication-competent viruses with functional Env’s were obtained when just the V1-V5 regions of these same A/D recombinants (i.e. same A/D breakpoints as above) were cloned into NL4-3. Conclusion These findings on functional A/D Env recombinants combined with structural models of Env suggest a conserved interplay between the C1 domain with C5 domain of gp120 and extracellular domain of gp41. Models also reveal a co-evolution within C1, C5, and ecto-gp41 domains which might explain the paucity of intersubtype recombination in the gp120 V1-V5 regions, despite their hypervariability. At least HIV-1 A/D intersubtype recombination in gp120 may result in a C1 from one subtype incompatible with a C5/gp41 from another subtype.
-
Functional bottlenecks for generation of HIV-1 intersubtype Env recombinants
Retrovirology, 2015Co-Authors: Bernard S. Bagaya, José F. Vega, Meijuan Tian, Kendall C. Krebs, Eric J. Arts, Gabrielle Nickel, Yong GaoAbstract:Intersubtype recombination is a powerful driving force for HIV evolution, impacting both HIV-1 diversity within an infected individual and within the global epidemic. This study examines if Viral Protein function/fitness is the major constraint shaping selection of recombination hotspots in replication-competent HIV-1 progeny. A better understanding of the interplay between Viral Protein Structure-function and recombination may provide insights into both vaccine design and drug development. In vitro HIV-1 dual infections were used to recombine subtypes A and D isolates and examine breakpoints in the Env glycoProteins. The entire env genes of 21 A/D recombinants with breakpoints in gp120 were non-functional when cloned into the laboratory strain, NL4-3. Likewise, cloning of A/D gp120 coding regions also produced dead viruses with non-functional Envs. 4/9 replication-competent viruses with functional Env’s were obtained when just the V1-V5 regions of these same A/D recombinants (i.e. same A/D breakpoints as above) were cloned into NL4-3. These findings on functional A/D Env recombinants combined with structural models of Env suggest a conserved interplay between the C1 domain with C5 domain of gp120 and extracellular domain of gp41. Models also reveal a co-evolution within C1, C5, and ecto-gp41 domains which might explain the paucity of intersubtype recombination in the gp120 V1-V5 regions, despite their hypervariability. At least HIV-1 A/D intersubtype recombination in gp120 may result in a C1 from one subtype incompatible with a C5/gp41 from another subtype.
Maud Sorel - One of the best experts on this subject based on the ideXlab platform.
-
The Potyviridae Cylindrical Inclusion helicase: a key multipartner and multifunctional Protein
Molecular Plant-Microbe Interactions, 2014Co-Authors: Maud Sorel, Juan Antonio García, Sylvie German-retanaAbstract:A unique feature shared by all plant viruses of the Potyviridae family is the induction of characteristic pinwheel-shaped inclusion bodies in the cytoplasm of infected cells. These cylindrical inclusions are composed of the Viral encoded cylindrical inclusion helicase (CI Protein). Its helicase activity was characterized and its involvement in replication demonstrated through different reverse genetics approaches. Beside replication, the CI Protein is also involved in cell-to-cell and long distance movements, possibly through interactions with the recently discovered Viral P3N-PIPO Protein. Studies over the past two decades demonstrate that the CI Protein is present in several cellular compartments interacting with Viral and plant Protein partners likely involved in its various roles in different steps of Viral infection. Furthermore, the CI Protein acts as an avirulence factor in gene for gene interaction with dominant-resistance host genes, and a recessive-resistance overcoming factor. Although a significant amount of data concerning the potential functions and subcellular localization of this Protein has been published, no synthetic review is available on this important multifunctional Protein. In this review, we compile and integrate all information relevant to the current understanding of this Viral Protein Structure and function and present a mode of action for CI, combining replication and movement.
-
The Potyviridae cylindrical inclusion helicase: a key multipartner and multifunctional Protein.
Molecular plant-microbe interactions : MPMI, 2014Co-Authors: Maud Sorel, Juan Antonio García, Sylvie German-retanaAbstract:A unique feature shared by all plant viruses of the Potyviridae family is the induction of characteristic pinwheel-shaped inclusion bodies in the cytoplasm of infected cells. These cylindrical inclusions are composed of the Viral-encoded cylindrical inclusion helicase (CI Protein). Its helicase activity was characterized and its involvement in replication demonstrated through different reverse genetics approaches. In addition to replication, the CI Protein is also involved in cell-to-cell and long-distance movements, possibly through interactions with the recently discovered Viral P3N-PIPO Protein. Studies over the past two decades demonstrate that the CI Protein is present in several cellular compartments interacting with Viral and plant Protein partners likely involved in its various roles in different steps of Viral infection. Furthermore, the CI Protein acts as an avirulence factor in gene-for-gene interactions with dominant-resistance host genes and as a recessive-resistance overcoming factor. Although a significant amount of data concerning the potential functions and subcellular localization of this Protein has been published, no synthetic review is available on this important multifunctional Protein. In this review, we compile and integrate all information relevant to the current understanding of this Viral Protein Structure and function and present a mode of action for CI, combining replication and movement.
Eric J. Arts - One of the best experts on this subject based on the ideXlab platform.
-
Functional bottlenecks for generation of HIV-1 intersubtype Env recombinants
Retrovirology, 2015Co-Authors: Bernard S. Bagaya, José F. Vega, Meijuan Tian, Gabrielle C. Nickel, Kendall C. Krebs, Eric J. Arts, Yong GaoAbstract:Background Intersubtype recombination is a powerful driving force for HIV evolution, impacting both HIV-1 diversity within an infected individual and within the global epidemic. This study examines if Viral Protein function/fitness is the major constraint shaping selection of recombination hotspots in replication-competent HIV-1 progeny. A better understanding of the interplay between Viral Protein Structure-function and recombination may provide insights into both vaccine design and drug development. Results In vitro HIV-1 dual infections were used to recombine subtypes A and D isolates and examine breakpoints in the Env glycoProteins. The entire env genes of 21 A/D recombinants with breakpoints in gp120 were non-functional when cloned into the laboratory strain, NL4-3. Likewise, cloning of A/D gp120 coding regions also produced dead viruses with non-functional Envs. 4/9 replication-competent viruses with functional Env’s were obtained when just the V1-V5 regions of these same A/D recombinants (i.e. same A/D breakpoints as above) were cloned into NL4-3. Conclusion These findings on functional A/D Env recombinants combined with structural models of Env suggest a conserved interplay between the C1 domain with C5 domain of gp120 and extracellular domain of gp41. Models also reveal a co-evolution within C1, C5, and ecto-gp41 domains which might explain the paucity of intersubtype recombination in the gp120 V1-V5 regions, despite their hypervariability. At least HIV-1 A/D intersubtype recombination in gp120 may result in a C1 from one subtype incompatible with a C5/gp41 from another subtype.
-
Functional bottlenecks for generation of HIV-1 intersubtype Env recombinants
Retrovirology, 2015Co-Authors: Bernard S. Bagaya, José F. Vega, Meijuan Tian, Kendall C. Krebs, Eric J. Arts, Gabrielle Nickel, Yong GaoAbstract:Intersubtype recombination is a powerful driving force for HIV evolution, impacting both HIV-1 diversity within an infected individual and within the global epidemic. This study examines if Viral Protein function/fitness is the major constraint shaping selection of recombination hotspots in replication-competent HIV-1 progeny. A better understanding of the interplay between Viral Protein Structure-function and recombination may provide insights into both vaccine design and drug development. In vitro HIV-1 dual infections were used to recombine subtypes A and D isolates and examine breakpoints in the Env glycoProteins. The entire env genes of 21 A/D recombinants with breakpoints in gp120 were non-functional when cloned into the laboratory strain, NL4-3. Likewise, cloning of A/D gp120 coding regions also produced dead viruses with non-functional Envs. 4/9 replication-competent viruses with functional Env’s were obtained when just the V1-V5 regions of these same A/D recombinants (i.e. same A/D breakpoints as above) were cloned into NL4-3. These findings on functional A/D Env recombinants combined with structural models of Env suggest a conserved interplay between the C1 domain with C5 domain of gp120 and extracellular domain of gp41. Models also reveal a co-evolution within C1, C5, and ecto-gp41 domains which might explain the paucity of intersubtype recombination in the gp120 V1-V5 regions, despite their hypervariability. At least HIV-1 A/D intersubtype recombination in gp120 may result in a C1 from one subtype incompatible with a C5/gp41 from another subtype.
