Search

Your search keyword '"Molshanski-Mor, Shahar"' showing total 28 results
Start Over Author "Molshanski-Mor, Shahar"
28 results on '"Molshanski-Mor, Shahar"'

3. Global phylogeography and ancient evolution of the widespread human gut virus crAssphage

Author

Edwards, Robert A., Vega, Alejandro A., Norman, Holly M., Ohaeri, Maria, Levi, Kyle, Dinsdale, Elizabeth A., Cinek, Ondrej, Aziz, Ramy K., McNair, Katelyn, Barr, Jeremy J., Bibby, Kyle, Brouns, Stan J. J., Cazares, Adrian, de Jonge, Patrick A., Desnues, Christelle, Díaz Muñoz, Samuel L., Fineran, Peter C., Kurilshikov, Alexander, Lavigne, Rob, Mazankova, Karla, McCarthy, David T., Nobrega, Franklin L., Reyes Muñoz, Alejandro, Tapia, German, Trefault, Nicole, Tyakht, Alexander V., Vinuesa, Pablo, Wagemans, Jeroen, Zhernakova, Alexandra, Aarestrup, Frank M., Ahmadov, Gunduz, Alassaf, Abeer, Anton, Josefa, Asangba, Abigail, Billings, Emma K., Cantu, Vito Adrian, Carlton, Jane M., Cazares, Daniel, Cho, Gyu-Sung, Condeff, Tess, Cortés, Pilar, Cranfield, Mike, Cuevas, Daniel A., De la Iglesia, Rodrigo, Decewicz, Przemyslaw, Doane, Michael P., Dominy, Nathaniel J., Dziewit, Lukasz, Elwasila, Bashir Mukhtar, Eren, A. Murat, Franz, Charles, Fu, Jingyuan, Garcia-Aljaro, Cristina, Ghedin, Elodie, Gulino, Kristen M., Haggerty, John M., Head, Steven R., Hendriksen, Rene S., Hill, Colin, Hyöty, Heikki, Ilina, Elena N., Irwin, Mitchell T., Jeffries, Thomas C., Jofre, Juan, Junge, Randall E., Kelley, Scott T., Khan Mirzaei, Mohammadali, Kowalewski, Martin, Kumaresan, Deepak, Leigh, Steven R., Lipson, David, Lisitsyna, Eugenia S., Llagostera, Montserrat, Maritz, Julia M., Marr, Linsey C., McCann, Angela, Molshanski-Mor, Shahar, Monteiro, Silvia, Moreira-Grez, Benjamin, Morris, Megan, Mugisha, Lawrence, Muniesa, Maite, Neve, Horst, Nguyen, Nam-phuong, Nigro, Olivia D., Nilsson, Anders S., O’Connell, Taylor, Odeh, Rasha, Oliver, Andrew, Piuri, Mariana, Prussin II, Aaron J., Qimron, Udi, Quan, Zhe-Xue, Rainetova, Petra, Ramírez-Rojas, Adán, Raya, Raul, Reasor, Kim, Rice, Gillian A. O., Rossi, Alessandro, Santos, Ricardo, Shimashita, John, Stachler, Elyse N., Stene, Lars C., Strain, Ronan, Stumpf, Rebecca, Torres, Pedro J., Twaddle, Alan, Ugochi Ibekwe, MaryAnn, Villagra, Nicolás, Wandro, Stephen, White, Bryan, Whiteley, Andy, Whiteson, Katrine L., Wijmenga, Cisca, Zambrano, Maria M., Zschach, Henrike, and Dutilh, Bas E.

Published
2019
Full Text
View/download PDF

7. No single irreplaceable acidic residues in the Escherichia coli secondary multidrug transporter MdfA

Author

Sigal, Nadejda, Molshanski-Mor, Shahar, and Bibi, Eitan

Subjects
Escherichia coli -- Genetic aspects, Biological sciences
Abstract

The largest family of solute transporters (major facilitator superfamily [MFS]) includes proton-motive-force-driven secondary transporters. Several characterized MFS transporters utilize essential acidic residues that play a critical role in the energy-coupling mechanism during transport. Surprisingly, we show here that no single acidic residue plays an irreplaceable role in the Escherichia coli secondary multidrug transporter MdfA.

Published
2006

8. 3D model of the escherichia coli multidrug transporter MdfA reveals an essential membrane-embedded positive charge

Author

Sigal, Nadejda, Vardy, Eyal, Molshanski-Mor, Shahar, Eitan, Asa, Pilpel, Yitzhak, Schuldiner, Shimon, and Bibi, Eitan

Subjects
Escherichia coli -- Research, Cell membranes -- Chemical properties, Membrane proteins -- Chemical properties, Biological sciences, Chemistry
Abstract

A study of secondary Mdr (multidrug resistance) transport was conducted by taking MdfA, which is an Escherichia (E.) coli, an Mdr transporter as a model. It showed that MdfA has a complex multidrug recognition pocket with exceptional capabilities for interacting with neutral and positively charged compounds.

Published
2005

9. Cell-Free Assays

Author

Molshanski-Mor, Shahar, primary, Mizrahi, Ariel, additional, Ugolev, Yelena, additional, Dahan, Iris, additional, Berdichevsky, Yevgeny, additional, and Pick, Edgar, additional

Published
2007
Full Text
View/download PDF

10. Global phylogeography and ancient evolution of the widespread human gut virus crAssphage

Author

Edwards, Robert A, Vega, Alejandro A, Norman, Holly M, Ohaeri, Maria, Levi, Kyle, Dinsdale, Elizabeth A, Cinek, Ondrej, Aziz, Ramy K, McNair, Katelyn, Barr, Jeremy J, Bibby, Kyle, Brouns, Stan J J, Cazares, Adrian, de Jonge, Patrick A, Desnues, Christelle, Díaz Muñoz, Samuel L, Fineran, Peter C, Kurilshikov, Alexander, Lavigne, Rob, Mazankova, Karla, McCarthy, David T, Nobrega, Franklin L, Reyes Muñoz, Alejandro, Tapia, German, Trefault, Nicole, Tyakht, Alexander V, Vinuesa, Pablo, Wagemans, Jeroen, Zhernakova, Alexandra, Aarestrup, Frank M, Ahmadov, Gunduz, Alassaf, Abeer, Anton, Josefa, Asangba, Abigail, Billings, Emma K, Cantu, Vito Adrian, Carlton, Jane M, Cazares, Daniel, Cho, Gyu-Sung, Condeff, Tess, Cortés, Pilar, Cranfield, Mike, Cuevas, Daniel A, De la Iglesia, Rodrigo, Decewicz, Przemyslaw, Doane, Michael P, Dominy, Nathaniel J, Dziewit, Lukasz, Elwasila, Bashir Mukhtar, Eren, A Murat, Franz, Charles, Fu, Jingyuan, Garcia-Aljaro, Cristina, Ghedin, Elodie, Gulino, Kristen M, Haggerty, John M, Head, Steven R, Hendriksen, Rene S, Hill, Colin, Hyöty, Heikki, Ilina, Elena N, Irwin, Mitchell T, Jeffries, Thomas C, Jofre, Juan, Junge, Randall E, Kelley, Scott T, Khan Mirzaei, Mohammadali, Kowalewski, Martin, Kumaresan, Deepak, Leigh, Steven R, Lipson, David, Lisitsyna, Eugenia S, Llagostera, Montserrat, Maritz, Julia M, Marr, Linsey C, McCann, Angela, Molshanski-Mor, Shahar, Monteiro, Silvia, Moreira-Grez, Benjamin, Morris, Megan, Mugisha, Lawrence, Muniesa, Maite, Neve, Horst, Nguyen, Nam-Phuong, Nigro, Olivia D, Nilsson, Anders S, O'Connell, Taylor, Odeh, Rasha, Oliver, Andrew, Piuri, Mariana, Prussin Ii, Aaron J, Qimron, Udi, Quan, Zhe-Xue, Rainetova, Petra, Ramírez-Rojas, Adán, Raya, Raul, Reasor, Kim, Rice, Gillian A O, Rossi, Alessandro, Santos, Ricardo, Shimashita, John, Stachler, Elyse N, Stene, Lars C, Strain, Ronan, Stumpf, Rebecca, Torres, Pedro J, Twaddle, Alan, Ugochi Ibekwe, MaryAnn, Villagra, Nicolás, Wandro, Stephen, White, Bryan, Whiteley, Andy, Whiteson, Katrine L, Wijmenga, Cisca, Zambrano, Maria M, Zschach, Henrike, Dutilh, Bas E, Edwards, Robert A, Vega, Alejandro A, Norman, Holly M, Ohaeri, Maria, Levi, Kyle, Dinsdale, Elizabeth A, Cinek, Ondrej, Aziz, Ramy K, McNair, Katelyn, Barr, Jeremy J, Bibby, Kyle, Brouns, Stan J J, Cazares, Adrian, de Jonge, Patrick A, Desnues, Christelle, Díaz Muñoz, Samuel L, Fineran, Peter C, Kurilshikov, Alexander, Lavigne, Rob, Mazankova, Karla, McCarthy, David T, Nobrega, Franklin L, Reyes Muñoz, Alejandro, Tapia, German, Trefault, Nicole, Tyakht, Alexander V, Vinuesa, Pablo, Wagemans, Jeroen, Zhernakova, Alexandra, Aarestrup, Frank M, Ahmadov, Gunduz, Alassaf, Abeer, Anton, Josefa, Asangba, Abigail, Billings, Emma K, Cantu, Vito Adrian, Carlton, Jane M, Cazares, Daniel, Cho, Gyu-Sung, Condeff, Tess, Cortés, Pilar, Cranfield, Mike, Cuevas, Daniel A, De la Iglesia, Rodrigo, Decewicz, Przemyslaw, Doane, Michael P, Dominy, Nathaniel J, Dziewit, Lukasz, Elwasila, Bashir Mukhtar, Eren, A Murat, Franz, Charles, Fu, Jingyuan, Garcia-Aljaro, Cristina, Ghedin, Elodie, Gulino, Kristen M, Haggerty, John M, Head, Steven R, Hendriksen, Rene S, Hill, Colin, Hyöty, Heikki, Ilina, Elena N, Irwin, Mitchell T, Jeffries, Thomas C, Jofre, Juan, Junge, Randall E, Kelley, Scott T, Khan Mirzaei, Mohammadali, Kowalewski, Martin, Kumaresan, Deepak, Leigh, Steven R, Lipson, David, Lisitsyna, Eugenia S, Llagostera, Montserrat, Maritz, Julia M, Marr, Linsey C, McCann, Angela, Molshanski-Mor, Shahar, Monteiro, Silvia, Moreira-Grez, Benjamin, Morris, Megan, Mugisha, Lawrence, Muniesa, Maite, Neve, Horst, Nguyen, Nam-Phuong, Nigro, Olivia D, Nilsson, Anders S, O'Connell, Taylor, Odeh, Rasha, Oliver, Andrew, Piuri, Mariana, Prussin Ii, Aaron J, Qimron, Udi, Quan, Zhe-Xue, Rainetova, Petra, Ramírez-Rojas, Adán, Raya, Raul, Reasor, Kim, Rice, Gillian A O, Rossi, Alessandro, Santos, Ricardo, Shimashita, John, Stachler, Elyse N, Stene, Lars C, Strain, Ronan, Stumpf, Rebecca, Torres, Pedro J, Twaddle, Alan, Ugochi Ibekwe, MaryAnn, Villagra, Nicolás, Wandro, Stephen, White, Bryan, Whiteley, Andy, Whiteson, Katrine L, Wijmenga, Cisca, Zambrano, Maria M, Zschach, Henrike, and Dutilh, Bas E

Abstract

Microbiomes are vast communities of microorganisms and viruses that populate all natural ecosystems. Viruses have been considered to be the most variable component of microbiomes, as supported by virome surveys and examples of high genomic mosaicism. However, recent evidence suggests that the human gut virome is remarkably stable compared with that of other environments. Here, we investigate the origin, evolution and epidemiology of crAssphage, a widespread human gut virus. Through a global collaboration, we obtained DNA sequences of crAssphage from more than one-third of the world's countries and showed that the phylogeography of crAssphage is locally clustered within countries, cities and individuals. We also found fully colinear crAssphage-like genomes in both Old-World and New-World primates, suggesting that the association of crAssphage with primates may be millions of years old. Finally, by exploiting a large cohort of more than 1,000 individuals, we tested whether crAssphage is associated with bacterial taxonomic groups of the gut microbiome, diverse human health parameters and a wide range of dietary factors. We identified strong correlations with different clades of bacteria that are related to Bacteroidetes and weak associations with several diet categories, but no significant association with health or disease. We conclude that crAssphage is a benign cosmopolitan virus that may have coevolved with the human lineage and is an integral part of the normal human gut virome.

Published
2019

11. Global phylogeography and ancient evolution of the widespread human gut virus crAssphage

Author

Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología, Edwards, Robert A., Vega, Alejandro A., Norman, Holly M., Ohaeri, Maria, Levi, Kyle, Dinsdale, Elizabeth A., Cinek, Ondrej, Aziz, Ramy K., McNair, Katelyn, Barr, Jeremy J., Bibby, Kyle, Shimashita, John, Stachler, Elyse N., Stene, Lars C., Strain, Ronan, Stumpf, Rebecca, Torres, Pedro J., Twaddle, Alan, Ugochi Ibekwe, MaryAnn, Villagra, Nicolás, Wandro, Stephen, Brouns, Stan J.J., White, Bryan, Whiteley, Andy, Whiteson, Katrine L., Wijmenga, Cisca, Zambrano, Maria M., Zschach, Henrike, Dutilh, Bas E., Cazares, Adrian, Jonge, Patrick A. de, Desnues, Christelle, Díaz Muñoz, Samuel L., Fineran, Peter C., Kurilshikov, Alexander, Lavigne, Rob, Mazankova, Karla, McCarthy, David T., Nobrega, Franklin L., Reyes Muñoz, Alejandro, Tapia, German, Trefault, Nicole, Tyakht, Alexander V., Vinuesa, Pablo, Wagemans, Jeroen, Zhernakova, Alexandra, Aarestrup, Frank M., Ahmadov, Gunduz, Alassaf, Abeer, Anton, Josefa, Asangba, Abigail, Billings, Emma K., Cantu, Vito Adrian, Carlton, Jane M., Cazares, Daniel, Cho, Gyu-Sung, Condeff, Tess, Cortés, Pilar, Cranfield, Mike, Cuevas, Daniel A., De la Iglesia, Rodrigo, Decewicz, Przemyslaw, Doane, Michael P., Dominy, Nathaniel J., Dziewit, Lukasz, Elwasila, Bashir Mukhtar, Eren, A. Murat, Franz, Charles, Fu, Jingyuan, Garcia-Aljaro, Cristina, Ghedin, Elodie, Gulino, Kristen M., Haggerty, John M., Head, Steven R., Hendriksen, Rene S., Hill, Colin, Hyöty, Heikki, Ilina, Elena N., Irwin, Mitchell T., Jeffries, Thomas C., Jofre, Juan, Junge, Randall E., Kelley, Scott T., Mirzaei, Mohammadali Khan, Kowalewski, Martin, Kumaresan, Deepak, Leigh, Steven R., Lipson, David, Lisitsyna, Eugenia S., Llagostera, Montserrat, Maritz, Julia M., Marr, Linsey C., McCann, Angela, Molshanski-Mor, Shahar, Monteiro, Silvia, Moreira-Grez, Benjamin, Morris, Megan, Mugisha, Lawrence, Muniesa, Maite, Neve, Horst, Nguyen, Nam-phuong, Nigro, Olivia D., Nilsson, Anders S., O’Connell, Taylor, Odeh, Rasha, Oliver, Andrew, Piuri, Mariana, Prussin II, Aaron J., Qimron, Udi, Quan, Zhe-Xue, Rainetova, Petra, Ramírez-Rojas, Adán, Raya, Raul, Reasor, Kim, Rice, Gillian A.O., Rossi, Alessandro, Santos, Ricardo, Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología, Edwards, Robert A., Vega, Alejandro A., Norman, Holly M., Ohaeri, Maria, Levi, Kyle, Dinsdale, Elizabeth A., Cinek, Ondrej, Aziz, Ramy K., McNair, Katelyn, Barr, Jeremy J., Bibby, Kyle, Shimashita, John, Stachler, Elyse N., Stene, Lars C., Strain, Ronan, Stumpf, Rebecca, Torres, Pedro J., Twaddle, Alan, Ugochi Ibekwe, MaryAnn, Villagra, Nicolás, Wandro, Stephen, Brouns, Stan J.J., White, Bryan, Whiteley, Andy, Whiteson, Katrine L., Wijmenga, Cisca, Zambrano, Maria M., Zschach, Henrike, Dutilh, Bas E., Cazares, Adrian, Jonge, Patrick A. de, Desnues, Christelle, Díaz Muñoz, Samuel L., Fineran, Peter C., Kurilshikov, Alexander, Lavigne, Rob, Mazankova, Karla, McCarthy, David T., Nobrega, Franklin L., Reyes Muñoz, Alejandro, Tapia, German, Trefault, Nicole, Tyakht, Alexander V., Vinuesa, Pablo, Wagemans, Jeroen, Zhernakova, Alexandra, Aarestrup, Frank M., Ahmadov, Gunduz, Alassaf, Abeer, Anton, Josefa, Asangba, Abigail, Billings, Emma K., Cantu, Vito Adrian, Carlton, Jane M., Cazares, Daniel, Cho, Gyu-Sung, Condeff, Tess, Cortés, Pilar, Cranfield, Mike, Cuevas, Daniel A., De la Iglesia, Rodrigo, Decewicz, Przemyslaw, Doane, Michael P., Dominy, Nathaniel J., Dziewit, Lukasz, Elwasila, Bashir Mukhtar, Eren, A. Murat, Franz, Charles, Fu, Jingyuan, Garcia-Aljaro, Cristina, Ghedin, Elodie, Gulino, Kristen M., Haggerty, John M., Head, Steven R., Hendriksen, Rene S., Hill, Colin, Hyöty, Heikki, Ilina, Elena N., Irwin, Mitchell T., Jeffries, Thomas C., Jofre, Juan, Junge, Randall E., Kelley, Scott T., Mirzaei, Mohammadali Khan, Kowalewski, Martin, Kumaresan, Deepak, Leigh, Steven R., Lipson, David, Lisitsyna, Eugenia S., Llagostera, Montserrat, Maritz, Julia M., Marr, Linsey C., McCann, Angela, Molshanski-Mor, Shahar, Monteiro, Silvia, Moreira-Grez, Benjamin, Morris, Megan, Mugisha, Lawrence, Muniesa, Maite, Neve, Horst, Nguyen, Nam-phuong, Nigro, Olivia D., Nilsson, Anders S., O’Connell, Taylor, Odeh, Rasha, Oliver, Andrew, Piuri, Mariana, Prussin II, Aaron J., Qimron, Udi, Quan, Zhe-Xue, Rainetova, Petra, Ramírez-Rojas, Adán, Raya, Raul, Reasor, Kim, Rice, Gillian A.O., Rossi, Alessandro, and Santos, Ricardo

Abstract

Microbiomes are vast communities of microorganisms and viruses that populate all natural ecosystems. Viruses have been considered to be the most variable component of microbiomes, as supported by virome surveys and examples of high genomic mosaicism. However, recent evidence suggests that the human gut virome is remarkably stable compared with that of other environments. Here, we investigate the origin, evolution and epidemiology of crAssphage, a widespread human gut virus. Through a global collaboration, we obtained DNA sequences of crAssphage from more than one-third of the world’s countries and showed that the phylogeography of crAssphage is locally clustered within countries, cities and individuals. We also found fully colinear crAssphage-like genomes in both Old-World and New-World primates, suggesting that the association of crAssphage with primates may be millions of years old. Finally, by exploiting a large cohort of more than 1,000 individuals, we tested whether crAssphage is associated with bacterial taxonomic groups of the gut microbiome, diverse human health parameters and a wide range of dietary factors. We identified strong correlations with different clades of bacteria that are related to Bacteroidetes and weak associations with several diet categories, but no significant association with health or disease. We conclude that crAssphage is a benign cosmopolitan virus that may have coevolved with the human lineage and is an integral part of the normal human gut virome.

Published
2019

12. Global phylogeography and ancient evolution of the widespread human gut virus crAssphage

Author

Theoretical Biology and Bioinformatics, Sub Bioinformatics, Edwards, Robert A, Vega, Alejandro A, Norman, Holly M, Ohaeri, Maria, Levi, Kyle, Dinsdale, Elizabeth A, Cinek, Ondrej, Aziz, Ramy K, McNair, Katelyn, Barr, Jeremy J, Bibby, Kyle, Brouns, Stan J J, Cazares, Adrian, de Jonge, Patrick A, Desnues, Christelle, Díaz Muñoz, Samuel L, Fineran, Peter C, Kurilshikov, Alexander, Lavigne, Rob, Mazankova, Karla, McCarthy, David T, Nobrega, Franklin L, Reyes Muñoz, Alejandro, Tapia, German, Trefault, Nicole, Tyakht, Alexander V, Vinuesa, Pablo, Wagemans, Jeroen, Zhernakova, Alexandra, Aarestrup, Frank M, Ahmadov, Gunduz, Alassaf, Abeer, Anton, Josefa, Asangba, Abigail, Billings, Emma K, Cantu, Vito Adrian, Carlton, Jane M, Cazares, Daniel, Cho, Gyu-Sung, Condeff, Tess, Cortés, Pilar, Cranfield, Mike, Cuevas, Daniel A, De la Iglesia, Rodrigo, Decewicz, Przemyslaw, Doane, Michael P, Dominy, Nathaniel J, Dziewit, Lukasz, Elwasila, Bashir Mukhtar, Eren, A Murat, Franz, Charles, Fu, Jingyuan, Garcia-Aljaro, Cristina, Ghedin, Elodie, Gulino, Kristen M, Haggerty, John M, Head, Steven R, Hendriksen, Rene S, Hill, Colin, Hyöty, Heikki, Ilina, Elena N, Irwin, Mitchell T, Jeffries, Thomas C, Jofre, Juan, Junge, Randall E, Kelley, Scott T, Khan Mirzaei, Mohammadali, Kowalewski, Martin, Kumaresan, Deepak, Leigh, Steven R, Lipson, David, Lisitsyna, Eugenia S, Llagostera, Montserrat, Maritz, Julia M, Marr, Linsey C, McCann, Angela, Molshanski-Mor, Shahar, Monteiro, Silvia, Moreira-Grez, Benjamin, Morris, Megan, Mugisha, Lawrence, Muniesa, Maite, Neve, Horst, Nguyen, Nam-Phuong, Nigro, Olivia D, Nilsson, Anders S, O'Connell, Taylor, Odeh, Rasha, Oliver, Andrew, Piuri, Mariana, Prussin Ii, Aaron J, Qimron, Udi, Quan, Zhe-Xue, Rainetova, Petra, Ramírez-Rojas, Adán, Raya, Raul, Reasor, Kim, Rice, Gillian A O, Rossi, Alessandro, Santos, Ricardo, Shimashita, John, Stachler, Elyse N, Stene, Lars C, Strain, Ronan, Stumpf, Rebecca, Torres, Pedro J, Twaddle, Alan, Ugochi Ibekwe, MaryAnn, Villagra, Nicolás, Wandro, Stephen, White, Bryan, Whiteley, Andy, Whiteson, Katrine L, Wijmenga, Cisca, Zambrano, Maria M, Zschach, Henrike, Dutilh, Bas E, Theoretical Biology and Bioinformatics, Sub Bioinformatics, Edwards, Robert A, Vega, Alejandro A, Norman, Holly M, Ohaeri, Maria, Levi, Kyle, Dinsdale, Elizabeth A, Cinek, Ondrej, Aziz, Ramy K, McNair, Katelyn, Barr, Jeremy J, Bibby, Kyle, Brouns, Stan J J, Cazares, Adrian, de Jonge, Patrick A, Desnues, Christelle, Díaz Muñoz, Samuel L, Fineran, Peter C, Kurilshikov, Alexander, Lavigne, Rob, Mazankova, Karla, McCarthy, David T, Nobrega, Franklin L, Reyes Muñoz, Alejandro, Tapia, German, Trefault, Nicole, Tyakht, Alexander V, Vinuesa, Pablo, Wagemans, Jeroen, Zhernakova, Alexandra, Aarestrup, Frank M, Ahmadov, Gunduz, Alassaf, Abeer, Anton, Josefa, Asangba, Abigail, Billings, Emma K, Cantu, Vito Adrian, Carlton, Jane M, Cazares, Daniel, Cho, Gyu-Sung, Condeff, Tess, Cortés, Pilar, Cranfield, Mike, Cuevas, Daniel A, De la Iglesia, Rodrigo, Decewicz, Przemyslaw, Doane, Michael P, Dominy, Nathaniel J, Dziewit, Lukasz, Elwasila, Bashir Mukhtar, Eren, A Murat, Franz, Charles, Fu, Jingyuan, Garcia-Aljaro, Cristina, Ghedin, Elodie, Gulino, Kristen M, Haggerty, John M, Head, Steven R, Hendriksen, Rene S, Hill, Colin, Hyöty, Heikki, Ilina, Elena N, Irwin, Mitchell T, Jeffries, Thomas C, Jofre, Juan, Junge, Randall E, Kelley, Scott T, Khan Mirzaei, Mohammadali, Kowalewski, Martin, Kumaresan, Deepak, Leigh, Steven R, Lipson, David, Lisitsyna, Eugenia S, Llagostera, Montserrat, Maritz, Julia M, Marr, Linsey C, McCann, Angela, Molshanski-Mor, Shahar, Monteiro, Silvia, Moreira-Grez, Benjamin, Morris, Megan, Mugisha, Lawrence, Muniesa, Maite, Neve, Horst, Nguyen, Nam-Phuong, Nigro, Olivia D, Nilsson, Anders S, O'Connell, Taylor, Odeh, Rasha, Oliver, Andrew, Piuri, Mariana, Prussin Ii, Aaron J, Qimron, Udi, Quan, Zhe-Xue, Rainetova, Petra, Ramírez-Rojas, Adán, Raya, Raul, Reasor, Kim, Rice, Gillian A O, Rossi, Alessandro, Santos, Ricardo, Shimashita, John, Stachler, Elyse N, Stene, Lars C, Strain, Ronan, Stumpf, Rebecca, Torres, Pedro J, Twaddle, Alan, Ugochi Ibekwe, MaryAnn, Villagra, Nicolás, Wandro, Stephen, White, Bryan, Whiteley, Andy, Whiteson, Katrine L, Wijmenga, Cisca, Zambrano, Maria M, Zschach, Henrike, and Dutilh, Bas E

Published
2019

13. Global phylogeography and ancient evolution of the widespread human gut virus crAssphage

Author

Edwards, Robert, primary, Vega, Alejandro, additional, Norman, Holly, additional, Ohaeri, Maria Cynthia, additional, Levi, Kyle, additional, Dinsdale, Elizabeth, additional, Cinek, Ondrej, additional, Aziz, Ramy, additional, McNair, Katelyn, additional, Barr, Jeremy, additional, Bibby, Kyle, additional, Brouns, Stan, additional, Cazares, Adrian, additional, de Jonge, Patrick A., additional, Desnues, Christelle, additional, Diaz-Munoz, Samuel, additional, Fineran, Peter, additional, Kurilshikov, Alexander, additional, Lavigne, Rob, additional, Mazankova, Karla, additional, McCarthy, David, additional, Nobrega, Franklin, additional, Reyes, Alejandro, additional, Tapia, German, additional, Trefault, Nicole, additional, Tyakht, Alexander, additional, Vinuesa, Pablo, additional, Wagemans, Jeroen, additional, Zhernakova, Alexandra, additional, Aarestrup, Frank, additional, Ahmadov, Gunduz, additional, Alassaf, Abeer, additional, Anton, Josefa, additional, Asangba, Abigail, additional, Billings, Emma, additional, Cantu, Adrian, additional, Carlton, Jane, additional, Cazares Lopez, Daniel, additional, Cho, Gyu-Sung, additional, Condeff, Tess, additional, Cortes, Pilar, additional, Cranfield, Micheal, additional, Cuevas, Daniel, additional, De la Iglesia, Rodrigo, additional, Decewicz, Przemyslaw, additional, Doane, Michael, additional, Dominy, Nathaniel, additional, Dziewit, Lukasz, additional, Elmahi, Bashir, additional, Eren, Murat, additional, Franz, Charles, additional, Fu, Jingyuan, additional, Garcia-Aljaro, Cristina, additional, Ghedin, Elodie, additional, Gulino, Kristen, additional, Haggerty, John, additional, Head, Steven, additional, Hendriksen, Rene S., additional, Hill, Colin, additional, Hyoty, Heikki, additional, Ilina, Elena, additional, Irwin, Mitchell, additional, Jeffries, Thomas, additional, Jofre, Juan, additional, Junge, Randall, additional, Kelley, Scott, additional, Kowalewski, Martin, additional, Kumaresan, Deepak, additional, Leigh, Steven, additional, Lisitsyna, Eugenia, additional, Llagostera, Montserrat, additional, Maritz, Julia M., additional, Marr, Linsey, additional, McCann, Angela, additional, Khan Mirzaei, Mohammadali, additional, Molshanski-Mor, Shahar, additional, Monteiro, Silvia, additional, Moreira-Grez, Benjamin, additional, Morris, Megan, additional, Mugisha, Lawrence, additional, Muniesa, Maite, additional, Neve, Horst, additional, Nguyen, Nam-phuong, additional, Nigro, Olivia, additional, Nilsson, Anders, additional, O'Connell, Taylor, additional, Odeh, Rasha, additional, Oliver, Andrew, additional, Piuri, Mariana, additional, Prussin, Aaron, additional, Qimron, Udi, additional, Quan, Zhe-Xue, additional, Rainetova, Petra, additional, Ramirez-Rojas, Adan, additional, Raya, Raul, additional, Rice, Gillian, additional, Rossi, Alessandro, additional, Santos, Ricardo, additional, Shimashita, John, additional, Stachler, Elyse, additional, Stene, Lars, additional, Strain, Ronan, additional, Stumpf, Rebecca, additional, Torres, Pedro, additional, Twaddle, Alan, additional, Ibekwe, Maryann Ugochi, additional, Villagra, Nicolas, additional, Wandro, Stephen, additional, White, Bryan, additional, Whiteley, Andrew, additional, Whiteson, Katrine, additional, Wijmenga, Cisca, additional, Zambrano, Maria Mercedes, additional, Zschach, Henrike, additional, and Dutilh, Bas E., additional

Published
2019
Full Text
View/download PDF

20. Assembly of the phagocyte NADPH oxidase complex: chimeric constructs derived from the cytosolic components as tools for exploring structure-function relationships

Author

Mizrahi, Ariel, primary, Berdichevsky, Yevgeny, additional, Ugolev, Yelena, additional, Molshanski-Mor, Shahar, additional, Nakash, Yael, additional, Dahan, Iris, additional, Alloul, Nathalie, additional, Gorzalczany, Yara, additional, Sarfstein, Rive, additional, Hirshberg, Miriam, additional, and Pick, Edgar, additional

Published
2006
Full Text
View/download PDF

23. Cell-Free Assays.

Author

Walker, John M., Quinn, Mark T., DeLeo, Frank R., Bokoch, Gary M., Molshanski-Mor, Shahar, Mizrahi, Ariel, Ugolev, Yelena, Dahan, Iris, Berdichevsky, Yevgeny, and Pick, Edgar

Abstract

The superoxide (O2•−)-generating enzyme complex of phagocytes, known as the NADPH oxidase, can be assayed in a number of in vitro cell-free (or broken cell) systems. These consist of a mixture of the individual components of the NADPH oxidase, derived from resting phagocytes or in the form of purified recombinant proteins, exposed to an activating agent (or situation), in the presence of NADPH and oxygen. O2•− produced by the mixture is measured by being trapped immediately after its generation with an appropriate acceptor in a kinetic assay, which permits the calculation of the linear rate of O2•− production over time. Cell-free assays are distinguished from whole-cell assays or assays performed on membranes derived from stimulated cells by the fact that all components in the reaction are derived from resting, nonstimulated cells and, thus, the steps of NADPH oxidase activation (precatalytic [assembly] and catalytic) occur in vitro. Cell-free assays played a paramount role in the identification of the components of the NADPH oxidase complex, the diagnosis of various forms of chronic granulomatous disease (CGD), and, more recently, the analysis of the domains present on the components of the NADPH oxidase participating in protein-protein interactions leading to the assembly of the active complex. [ABSTRACT FROM AUTHOR]

Published
2007
Full Text
View/download PDF

24. Inhibition of NADPH oxidase activation by peptides mapping within the dehydrogenase region of Nox2‐A “peptide walking” study

Author

Dahan, Iris, Molshanski‐Mor, Shahar, and Pick, Edgar

Abstract

Synthetic peptides corresponding to specific domains in the Nox2 dehydrogenase region inhibit NADPH oxidase activity in vitro by interfering with FAD‐ and NADPH‐related redox reactions. In this study, the “peptide walking” approach was applied to the DH region of Nox2 (residues 288–570) with the purpose of identifying domains of functional importance in the assembly and/or catalytic function of the NADPH oxidase complex of phagocytes. Ninety‐one overlapping 15‐mer peptides were synthesized to cover the full length of the Nox2 DH region, and these were tested for the ability to interfere with the activation of the oxidase in vitro in two semirecombinant cell‐free systems. The first consisted of phagocyte membranes p47phox, p67phox, and Rac1 and an amphiphile; the second was p47phox‐ and amphiphile‐free and contained prenylated Rac1. We identified 10 clusters of inhibitory peptides with IC50values of 10 μM, all of which were inhibitory, also in the absence of p47phox. Based on the identification of residues shared by peptides in a particular cluster, we defined 10 functional domains in the Nox2 DH region. One domain corresponded to one FAD‐binding subdomain, and four domains overlapped parts of three NADPH‐binding subdomains. As expected, most inhibitory peptides acted only when added prior to the completion of oxidase assembly, but peptides associated with two NADPH‐binding subdomains were also active after assembly. Kinetic analysis demonstrated that inhibition by peptides was not explained by competition for substrates (FAD, NADPH) but was of a more complex nature: noncompetitive with respect to FAD and uncompetitive with respect to NADPH. We conclude that oxidase‐inhibitory peptides, in five out of 10 clusters identified, act by interfering with FAD‐ and NADPH‐related redox reactions.

Published
2012
Full Text
View/download PDF

25. Tripartite Chimeras Comprising Functional Domains Derived from the Cytosolic NADPH Oxidase Components p47phox , p67phox, and Raci Elicit Activator-independent Superoxide Production by Phagocyte Membranes.

Author

Berdichevsky, Yevgeny, Mizrahi, Ariel, Ugolev, Yelena, Molshanski-Mor, Shahar, and Pick, Edgar

Subjects
*MOSAICISM, *OXIDASES, *SUPEROXIDES, *PHAGOCYTES, *CELL membranes, *CYTOCHROME b
Abstract

The superoxide-generating NADPH oxidase is converted to an active state by the assembly of a membrane-localized cytochrome b559 with three cytosolic components: p47phox, p67phox, and GTPase Rac1 or Rac2. Assembly involves two sets of protein-protein interactions: among cytosolic components and among cytosolic components and cytochrome b559 within its lipid habitat. We circumvented the need for interactions among cytosolic components by constructing a recombinant tripartite chimera (trimera) consisting of the Phox homology (PX) and Src homology 3 (SH3) domains of p47phox, the tetratricopeptide repeat and activation domains of p67phox, and full-length Rac1. Upon addition to phagocyte membrane, the trimera was capable of oxidase activation in vitro in the presence of an anionic amphiphile. The trimera had a higher affinity (lower EC50) for and formed a more stable complex (longer half-life) with cytochrome b559 compared with the combined individual components, full-length or truncated. Supplementation of membrane with anionic but not neutral phospholipids made activation by the trimera amphiphile-independent. Mutagenesis, truncations, and domain replacements revealed that oxidase activation by the trimera was dependent on the following interactions: 1) interaction with anionic membrane phospholipids via the poly-basic stretch at the C terminus of the Rac1 segment; 2) interaction with p22phox via Trp193 in the N-terminal SH3 domain of the p47phox segment, supplementing the electrostatic attraction; and 3) an intrachimeric bond among the p67phox and Rac1 segments complementary to their physical fusion. The PX domain of the p47phox segment and the insert domain of the Rac1 segment made only minor contributions to oxidase assembly. [ABSTRACT FROM AUTHOR]

Published
2007
Full Text
View/download PDF

26. Dual Role of Rac in the Assembly of NADPH Oxidase, Tethering to the Membrane and Activation of p67phox.

Author

Sarfstein, Rive, Gorzalczany, Yara, Mizrahi, Ariel, Berdichevsky, Yevgeny, Molshanski-Mor, Shahar, Weinbaum, Carolyn, Hirshberg, Miriam, Dagher, Marie-Claire, and Pick, Edgar

Subjects
*OXIDASES, *CYTOCHROME b, *GUANOSINE triphosphatase, *RAS proteins, *MOSAICISM, *BIOLOGICAL membranes
Abstract

NADPH oxidase activation involves the assembly of membrane-localized cytochrome b559 with the cytosolic components p47phox, p67phox, and the small GTPase Rac. Assembly is mimicked by a cell-free system consisting of membranes and cytosolic components, activated by an anionic amphiphile. We reported that a chimeric construct, consisting of residues 1-212 of p67phox and full-length Rac1, activates the oxidase in vitro in an amphiphile-dependent manner, and when prenylated, in the absence of amphiphile and p47phox. We subjected chimera p67phox-(1-212)-Rac1 to mutational analysis and found that: 1) replacement of a single basic residue at the C terminus of the Rac1 moiety by glutamine is sufficient for loss of activity by the non-prenylated chimera; replacement of all six basic residues by glutamines is required for loss of activity by the prenylated chimera. 2) A V204A mutation in the activation domain of the p67phox moiety leads to a reduction in activity. 3) Mutating residues, known to participate in the interaction between free p67phox and Rac1, in the p67phox(R102E) or Rac1 (A27K, G30S) moieties of the chimera, leads to a marked decrease in activity, indicating a requirement for intrachimeric bonds, in addition to the engineered fusion. 4) Chimeras, inactive because of mutations A27K or G30S in the Rac1 moiety, are reactivated by supplementation with exogenous Rac1-GTP but not with exogenous p67phox. This demonstrates that Rac has a dual role in the assembly of NADPH oxidase. One is to tether p67phox to the membrane; the other is to induce an "activating" conformational change in p67phox. [ABSTRACT FROM AUTHOR]

Published
2004
Full Text
View/download PDF

27. Cell-free assays: the reductionist approach to the study of NADPH oxidase assembly, or "all you wanted to know about cell-free assays but did not dare to ask".

Author

Molshanski-Mor S, Mizrahi A, Ugolev Y, Dahan I, Berdichevsky Y, and Pick E

Subjects
Animals, Catalysis, Cell Fractionation, Cell Membrane chemistry, Cell Membrane metabolism, Cell-Free System, Cytosol chemistry, Disposable Equipment, Humans, NADPH Oxidases metabolism, Phagocytes enzymology, Protein Binding, Sensitivity and Specificity, Multiprotein Complexes metabolism, NADPH Oxidases analysis
Abstract

The superoxide (O2-)-generating enzyme complex of phagocytes, known as the NADPH oxidase, can be assayed in a number of in vitro cell-free (or broken cell) systems. These consist of a mixture of the individual components of the NADPH oxidase, derived from resting phagocytes or in the form of purified recombinant proteins, exposed to an activating agent (or situation), in the presence of NADPH and oxygen. O2- produced by the mixture is measured by being trapped immediately after its generation with an appropriate acceptor in a kinetic assay, which permits the calculation of the linear rate of O2- production over time. Cell-free assays are distinguished from whole-cell assays or assays performed on membranes derived from stimulated cells by the fact that all components in the reaction are derived from resting, nonstimulated cells and, thus, the steps of NADPH oxidase activation (precatalytic [assembly] and catalytic) occur in vitro. Cell-free assays played a paramount role in the identification of the components of the NADPH oxidase complex, the diagnosis of various forms of chronic granulomatous disease (CGD), and, more recently, the analysis of the domains present on the components of the NADPH oxidase participating in protein-protein interactions leading to the assembly of the active complex.

Published
2007
Full Text
View/download PDF

28. Liposomes comprising anionic but not neutral phospholipids cause dissociation of Rac(1 or 2) x RhoGDI complexes and support amphiphile-independent NADPH oxidase activation by such complexes.

Author

Ugolev Y, Molshanski-Mor S, Weinbaum C, and Pick E

Subjects
Animals, Anions, Cytochrome b Group chemistry, Enzyme Activation, Guinea Pigs, Insecta, Phagocytes metabolism, Phosphoproteins metabolism, Photosystem II Protein Complex chemistry, Protein Transport, rho-Specific Guanine Nucleotide Dissociation Inhibitors, RAC2 GTP-Binding Protein, Guanine Nucleotide Dissociation Inhibitors chemistry, Liposomes chemistry, NADPH Oxidases chemistry, Phospholipids chemistry, rac GTP-Binding Proteins chemistry, rac1 GTP-Binding Protein chemistry
Abstract

Activation of the phagocyte NADPH oxidase involves the assembly of a membrane-localized cytochrome b559 with the cytosolic components p47(phox), p67(phox), p40(phox), and the GTPase Rac (1 or 2). In resting phagocytes, Rac is found in the cytosol as a prenylated protein in the GDP-bound form, associated with the Rho GDP dissociation inhibitor (RhoGDI). In the process of NADPH oxidase activation, Rac is dissociated from RhoGDI and translocates to the membrane, in concert with the other cytosolic components. The mechanism responsible for dissociation of Rac from RhoGDI is poorly understood. We generated Rac(1 or 2) x RhoGDI complexes in vitro from recombinant Rac(1 or 2), prenylated enzymatically, and recombinant RhoGDI, and purified these by anion exchange chromatography. Exposing Rac(1 or 2)(GDP) x RhoGDI complexes to liposomes containing four different anionic phospholipids caused the dissociation of Rac(1 or 2)(GDP) from RhoGDI and its binding to the anionic liposomes. Rac2(GDP) x RhoGDI complexes were more resistant to dissociation, reflecting the lesser positive charge of Rac2. Liposomes consisting of neutral phospholipid did not cause dissociation of Rac(1 or 2) x RhoGDI complexes. Rac1 exchanged to the hydrolysis-resistant GTP analogue, GMPPNP, associated with RhoGDI with lower affinity than Rac1(GDP) and Rac1(GMPPNP) x RhoGDI complexes were more readily dissociated by anionic liposomes. Rac1(GMPPNP) x RhoGDI complexes elicited NADPH oxidase activation in native phagocyte membrane liposomes in the presence of p67(phox), without the need for an anionic amphiphile, as activator. Both Rac1(GDP) x RhoGDI and Rac1(GMPPNP) x RhoGDI complexes elicited amphiphile-independent, p67(phox)-dependent NADPH oxidase activation in phagocyte membrane liposomes enriched in anionic phospholipids but not in membrane liposomes enriched in neutral phospholipids.

Published
2006
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results