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Comparison of serum hemagglutinin and neuraminidase inhibition antibodies after 2010-2011 trivalent inactivated influenza vaccination in healthcare personnel.

Open forum infectious diseases

Laguio-Vila MR, Thompson MG, Reynolds S, Spencer SM, Gaglani M, Naleway A, Ball S, Bozeman S, Baker S, Martínez-Sobrido L, Levine M, Katz J, Fry AM, Treanor JJ.
PMID: 25884004
Open Forum Infect Dis. 2015 Jan 03;2(1):ofu115. doi: 10.1093/ofid/ofu115. eCollection 2015 Jan.

Background.  Most inactivated influenza vaccines contain purified and standardized hemagglutinin (HA) and residual neuraminidase (NA) antigens. Vaccine-associated HA antibody responses (hemagglutination inhibition [HAI]) are well described, but less is known about the immune response to the NA. Methods.  Serum...

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Laguio-Vila MR, Thompson MG, Reynolds S, et al. Comparison of serum hemagglutinin and neuraminidase inhibition antibodies after 2010-2011 trivalent inactivated influenza vaccination in healthcare personnel. Open Forum Infect Dis. 2015;2(1):ofu115doi: 10.1093/ofid/ofu115.
Laguio-Vila, M. R., Thompson, M. G., Reynolds, S., Spencer, S. M., Gaglani, M., Naleway, A., Ball, S., Bozeman, S., Baker, S., Martínez-Sobrido, L., Levine, M., Katz, J., Fry, A. M., & Treanor, J. J. (2015). Comparison of serum hemagglutinin and neuraminidase inhibition antibodies after 2010-2011 trivalent inactivated influenza vaccination in healthcare personnel. Open forum infectious diseases, 2(1), ofu115. https://doi.org/10.1093/ofid/ofu115
Laguio-Vila, Maryrose R, et al. "Comparison of serum hemagglutinin and neuraminidase inhibition antibodies after 2010-2011 trivalent inactivated influenza vaccination in healthcare personnel." Open forum infectious diseases vol. 2,1 (2015): ofu115. doi: https://doi.org/10.1093/ofid/ofu115
Laguio-Vila MR, Thompson MG, Reynolds S, Spencer SM, Gaglani M, Naleway A, Ball S, Bozeman S, Baker S, Martínez-Sobrido L, Levine M, Katz J, Fry AM, Treanor JJ. Comparison of serum hemagglutinin and neuraminidase inhibition antibodies after 2010-2011 trivalent inactivated influenza vaccination in healthcare personnel. Open Forum Infect Dis. 2015 Jan 03;2(1):ofu115. doi: 10.1093/ofid/ofu115. eCollection 2015 Jan. PMID: 25884004; PMCID: PMC4396428.
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Influenza pH1N1 Virus Accumulated H275Y Mutation in Neuraminidase during Propagation in MDCK Cells.

Genome announcements

Mishel P, Bychkov D, Kallio-Kokko H, Valkonen M, Kantele A, Mattila P, Almusa H, Jalovaara P, Kainov D.
PMID: 25540354
Genome Announc. 2014 Dec 24;2(6). doi: 10.1128/genomeA.01349-14.

Here, we sequenced the genome of the influenza A/Finland/741 M/2014(H1N1) virus and found that the virus accumulated oseltamivir resistance mutation H275Y in its neuraminidase during propagation in cell culture. This indicates that propagation in cell culture modifies virus genomes....

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Mishel P, Bychkov D, Kallio-Kokko H, et al. Influenza pH1N1 Virus Accumulated H275Y Mutation in Neuraminidase during Propagation in MDCK Cells. Genome Announc. 2014;2(6)doi: 10.1128/genomeA.01349-14.
Mishel, P., Bychkov, D., Kallio-Kokko, H., Valkonen, M., Kantele, A., Mattila, P., Almusa, H., Jalovaara, P., & Kainov, D. (2014). Influenza pH1N1 Virus Accumulated H275Y Mutation in Neuraminidase during Propagation in MDCK Cells. Genome announcements, 2(6), . https://doi.org/10.1128/genomeA.01349-14
Mishel, Polina, et al. "Influenza pH1N1 Virus Accumulated H275Y Mutation in Neuraminidase during Propagation in MDCK Cells." Genome announcements vol. 2,6 (2014). doi: https://doi.org/10.1128/genomeA.01349-14
Mishel P, Bychkov D, Kallio-Kokko H, Valkonen M, Kantele A, Mattila P, Almusa H, Jalovaara P, Kainov D. Influenza pH1N1 Virus Accumulated H275Y Mutation in Neuraminidase during Propagation in MDCK Cells. Genome Announc. 2014 Dec 24;2(6). doi: 10.1128/genomeA.01349-14. PMID: 25540354; PMCID: PMC4276832.
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Predictors of mortality and length of stay in hospitalized cases of 2009 influenza A (H1N1): Experiences of a tertiary care center.

Indian journal of critical care medicine : peer-reviewed, official publication of Indian Society of Critical Care Medicine

Chawla R, Kansal S, Chauhan M, Jain A, Jibhkate BN.
PMID: 24339638
Indian J Crit Care Med. 2013 Sep;17(5):275-82. doi: 10.4103/0972-5229.120318.

AIM: To study the clinical characteristics and outcome of admitted patients of H1N1 (hemagglutinin -H neuraminidase -N) influenza in a tertiary level hospital, from Oct 2009 to Dec 2010.MATERIALS AND METHODS: A retrospective analysis of 77 confirmed patients admitted...

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Chawla R, Kansal S, Chauhan M, et al. Predictors of mortality and length of stay in hospitalized cases of 2009 influenza A (H1N1): Experiences of a tertiary care center. Indian J Crit Care Med. 2013;17(5):275-82doi: 10.4103/0972-5229.120318.
Chawla, R., Kansal, S., Chauhan, M., Jain, A., & Jibhkate, B. N. (2013). Predictors of mortality and length of stay in hospitalized cases of 2009 influenza A (H1N1): Experiences of a tertiary care center. Indian journal of critical care medicine : peer-reviewed, official publication of Indian Society of Critical Care Medicine, 17(5), 275-82. https://doi.org/10.4103/0972-5229.120318
Chawla, Rajesh, et al. "Predictors of mortality and length of stay in hospitalized cases of 2009 influenza A (H1N1): Experiences of a tertiary care center." Indian journal of critical care medicine : peer-reviewed, official publication of Indian Society of Critical Care Medicine vol. 17,5 (2013): 275-82. doi: https://doi.org/10.4103/0972-5229.120318
Chawla R, Kansal S, Chauhan M, Jain A, Jibhkate BN. Predictors of mortality and length of stay in hospitalized cases of 2009 influenza A (H1N1): Experiences of a tertiary care center. Indian J Crit Care Med. 2013 Sep;17(5):275-82. doi: 10.4103/0972-5229.120318. PMID: 24339638; PMCID: PMC3841489.
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Wheat germ cell-free system-based production of hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 for generation and characterization of monoclonal antibody.

Frontiers in microbiology

Matsunaga S, Kawakami S, Matsuo I, Okayama A, Tsukagoshi H, Kudoh A, Matsushima Y, Shimizu H, Okabe N, Hirano H, Yamamoto N, Kimura H, Ryo A.
PMID: 24860558
Front Microbiol. 2014 May 13;5:208. doi: 10.3389/fmicb.2014.00208. eCollection 2014.

Human parainfluenza virus 3 (HPIV3) commonly causes respiratory disorders in infants and young children. Monoclonal antibodies (MAbs) have been produced to several components of HPIV3 and commercially available. However, the utility of these antibodies for several immunological and proteomic...

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Matsunaga S, Kawakami S, Matsuo I, et al. Wheat germ cell-free system-based production of hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 for generation and characterization of monoclonal antibody. Front Microbiol. 2014;5:208doi: 10.3389/fmicb.2014.00208.
Matsunaga, S., Kawakami, S., Matsuo, I., Okayama, A., Tsukagoshi, H., Kudoh, A., Matsushima, Y., Shimizu, H., Okabe, N., Hirano, H., Yamamoto, N., Kimura, H., & Ryo, A. (2014). Wheat germ cell-free system-based production of hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 for generation and characterization of monoclonal antibody. Frontiers in microbiology, 5208. https://doi.org/10.3389/fmicb.2014.00208
Matsunaga, Satoko, et al. "Wheat germ cell-free system-based production of hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 for generation and characterization of monoclonal antibody." Frontiers in microbiology vol. 5 (2014): 208. doi: https://doi.org/10.3389/fmicb.2014.00208
Matsunaga S, Kawakami S, Matsuo I, Okayama A, Tsukagoshi H, Kudoh A, Matsushima Y, Shimizu H, Okabe N, Hirano H, Yamamoto N, Kimura H, Ryo A. Wheat germ cell-free system-based production of hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 for generation and characterization of monoclonal antibody. Front Microbiol. 2014 May 13;5:208. doi: 10.3389/fmicb.2014.00208. eCollection 2014. PMID: 24860558; PMCID: PMC4026691.
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Neuraminidase-1 mediates skeletal muscle regeneration.

Biochimica et biophysica acta

Neves Jde C, Rizzato VR, Fappi A, Garcia MM, Chadi G, van de Vlekkert D, d'Azzo A, Zanoteli E.
PMID: 26001931
Biochim Biophys Acta. 2015 Sep;1852(9):1755-64. doi: 10.1016/j.bbadis.2015.05.006. Epub 2015 May 19.

Neuraminidase-1 (NEU1) is the sialidase responsible for the catabolism of sialoglycoconjugates in lysosomes. Congenital NEU1 deficiency causes sialidosis, a severe lysosomal storage disease associated with a broad spectrum of clinical manifestations, which also include skeletal deformities, skeletal muscle hypotonia...

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Neves Jde C, Rizzato VR, Fappi A, et al. Neuraminidase-1 mediates skeletal muscle regeneration. Biochim Biophys Acta. 2015;1852(9):1755-64doi: 10.1016/j.bbadis.2015.05.006.
Neves, J. d. e. . C., Rizzato, V. R., Fappi, A., Garcia, M. M., Chadi, G., van de Vlekkert, D., d'Azzo, A., & Zanoteli, E. (2015). Neuraminidase-1 mediates skeletal muscle regeneration. Biochimica et biophysica acta, 1852(9), 1755-64. https://doi.org/10.1016/j.bbadis.2015.05.006
Neves, Juliana de Carvalho, et al. "Neuraminidase-1 mediates skeletal muscle regeneration." Biochimica et biophysica acta vol. 1852,9 (2015): 1755-64. doi: https://doi.org/10.1016/j.bbadis.2015.05.006
Neves Jde C, Rizzato VR, Fappi A, Garcia MM, Chadi G, van de Vlekkert D, d'Azzo A, Zanoteli E. Neuraminidase-1 mediates skeletal muscle regeneration. Biochim Biophys Acta. 2015 Sep;1852(9):1755-64. doi: 10.1016/j.bbadis.2015.05.006. Epub 2015 May 19. PMID: 26001931; PMCID: PMC5617636.
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Molecular docking of selected phytocompounds with H1N1 Proteins.

Bioinformation

Alhazmi MI.
PMID: 26124560
Bioinformation. 2015 Apr 30;11(4):196-202. doi: 10.6026/97320630011196. eCollection 2015.

The H1N1 influenza virus is a serious threat to human population. Oseltamivir and Zanamivir are known antiviral drugs for swine flu with observed side effects. These drugs are viral neuraminidase and hemagglutinin inhibitor prevents early virus multiplication by blocking...

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Alhazmi MI. Molecular docking of selected phytocompounds with H1N1 Proteins. Bioinformation. 2015;11(4):196-202doi: 10.6026/97320630011196.
Alhazmi, M. I. (2015). Molecular docking of selected phytocompounds with H1N1 Proteins. Bioinformation, 11(4), 196-202. https://doi.org/10.6026/97320630011196
Alhazmi, Mohammed I. "Molecular docking of selected phytocompounds with H1N1 Proteins." Bioinformation vol. 11,4 (2015): 196-202. doi: https://doi.org/10.6026/97320630011196
Alhazmi MI. Molecular docking of selected phytocompounds with H1N1 Proteins. Bioinformation. 2015 Apr 30;11(4):196-202. doi: 10.6026/97320630011196. eCollection 2015. PMID: 26124560; PMCID: PMC4479056.
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Construction of recombinant fusion protein of influenza, a virus neuraminidase and heat shock protein 70 gene: expression in baculovirus and bioactivity.

Journal of medicine and life

Moghaddam Pour M, Keivani H, Masoudi SH, Monavari SH, Najafi M.
PMID: 28316730
J Med Life. 2015;8:189-195.

No abstract available.

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Moghaddam Pour M, Keivani H, Masoudi SH, et al. Construction of recombinant fusion protein of influenza, a virus neuraminidase and heat shock protein 70 gene: expression in baculovirus and bioactivity. J Med Life. 2015;8:189-195
Moghaddam Pour, M., Keivani, H., Masoudi, S. H., Monavari, S. H., & Najafi, M. (2015). Construction of recombinant fusion protein of influenza, a virus neuraminidase and heat shock protein 70 gene: expression in baculovirus and bioactivity. Journal of medicine and life, 8189-195.
Moghaddam Pour, M, et al. "Construction of recombinant fusion protein of influenza, a virus neuraminidase and heat shock protein 70 gene: expression in baculovirus and bioactivity." Journal of medicine and life vol. 8 (2015): 189-195.
Moghaddam Pour M, Keivani H, Masoudi SH, Monavari SH, Najafi M. Construction of recombinant fusion protein of influenza, a virus neuraminidase and heat shock protein 70 gene: expression in baculovirus and bioactivity. J Med Life. 2015;8:189-195. PMID: 28316730; PMCID: PMC5319269.
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Epidemiological and viral genome characteristics of the first human H7N9 influenza infection in Guangdong Province, China.

Journal of thoracic disease

Yang ZF, He JF, Li XB, Guan WD, Ke CW, Wu SG, Pan SH, Li RF, Kang M, Wu J, Lin JY, Ding GY, Huang JC, Pan WQ, Zhou R, Lin YP, Chen RC, Li YM, Chen L, Xiao WL, Zhang YH, Zhong NS.
PMID: 25589974
J Thorac Dis. 2014 Dec;6(12):1785-93. doi: 10.3978/j.issn.2072-1439.2014.12.09.

BACKGROUND: The first H7N9 human case in south of China was confirmed in Guangdong Province on August 2013, outside of the typical influenza season. For investigating the H7N9 virus source and transmission in the local community, we analyze the...

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Yang ZF, He JF, Li XB, et al. Epidemiological and viral genome characteristics of the first human H7N9 influenza infection in Guangdong Province, China. J Thorac Dis. 2014;6(12):1785-93doi: 10.3978/j.issn.2072-1439.2014.12.09.
Yang, Z. F., He, J. F., Li, X. B., Guan, W. D., Ke, C. W., Wu, S. G., Pan, S. H., Li, R. F., Kang, M., Wu, J., Lin, J. Y., Ding, G. Y., Huang, J. C., Pan, W. Q., Zhou, R., Lin, Y. P., Chen, R. C., Li, Y. M., Chen, L., Xiao, W. L., Zhang, Y. H., & Zhong, N. S. (2014). Epidemiological and viral genome characteristics of the first human H7N9 influenza infection in Guangdong Province, China. Journal of thoracic disease, 6(12), 1785-93. https://doi.org/10.3978/j.issn.2072-1439.2014.12.09
Yang, Zi-Feng, et al. "Epidemiological and viral genome characteristics of the first human H7N9 influenza infection in Guangdong Province, China." Journal of thoracic disease vol. 6,12 (2014): 1785-93. doi: https://doi.org/10.3978/j.issn.2072-1439.2014.12.09
Yang ZF, He JF, Li XB, Guan WD, Ke CW, Wu SG, Pan SH, Li RF, Kang M, Wu J, Lin JY, Ding GY, Huang JC, Pan WQ, Zhou R, Lin YP, Chen RC, Li YM, Chen L, Xiao WL, Zhang YH, Zhong NS. Epidemiological and viral genome characteristics of the first human H7N9 influenza infection in Guangdong Province, China. J Thorac Dis. 2014 Dec;6(12):1785-93. doi: 10.3978/j.issn.2072-1439.2014.12.09. PMID: 25589974; PMCID: PMC4283329.
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Transcription and Translation of Sendai Virus Hemagglutinin-neuraminidase (HN) in Mammalian Cells.

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

Hu JH, Qi B, Nakanishi M, Qi YP.
PMID: 12075445
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2000;32(3):229-234.

Sendai virus hemagglutinin-neuraminidase was expressed in COS-7 cells. LLCMK(2) cells were transfected with expression plasmids harboring HN, namely pJH3, pJH4 or pJH7, and were passaged conti-nuously under the presence of hygromycin or puromycin to get antibiotic-resistant clones, which had...

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Hu JH, Qi B, Nakanishi M, et al. Transcription and Translation of Sendai Virus Hemagglutinin-neuraminidase (HN) in Mammalian Cells. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2000;32(3):229-234
Hu, J. H., Qi, B., Nakanishi, M., & Qi, Y. P. (2000). Transcription and Translation of Sendai Virus Hemagglutinin-neuraminidase (HN) in Mammalian Cells. Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica, 32(3), 229-234.
Hu, Jian-Hong, et al. "Transcription and Translation of Sendai Virus Hemagglutinin-neuraminidase (HN) in Mammalian Cells." Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica vol. 32,3 (2000): 229-234.
Hu JH, Qi B, Nakanishi M, Qi YP. Transcription and Translation of Sendai Virus Hemagglutinin-neuraminidase (HN) in Mammalian Cells. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2000;32(3):229-234. PMID: 12075445.
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Lysosomal hydrolases: Conversion of acidic to basic forms by neuraminidase.

FEBS letters

Goldstone A, Konecny P, Koenig H.
PMID: 11945635
FEBS Lett. 1971 Feb 12;13(1):68-72. doi: 10.1016/0014-5793(71)80667-1.

No abstract available.

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Goldstone A, Konecny P, Koenig H. Lysosomal hydrolases: Conversion of acidic to basic forms by neuraminidase. FEBS Lett. 1971;13(1):68-72doi: 10.1016/0014-5793(71)80667-1.
Goldstone, A., Konecny, P., & Koenig, H. (1971). Lysosomal hydrolases: Conversion of acidic to basic forms by neuraminidase. FEBS letters, 13(1), 68-72. https://doi.org/10.1016/0014-5793(71)80667-1
Goldstone, A, et al. "Lysosomal hydrolases: Conversion of acidic to basic forms by neuraminidase." FEBS letters vol. 13,1 (1971): 68-72. doi: https://doi.org/10.1016/0014-5793(71)80667-1
Goldstone A, Konecny P, Koenig H. Lysosomal hydrolases: Conversion of acidic to basic forms by neuraminidase. FEBS Lett. 1971 Feb 12;13(1):68-72. doi: 10.1016/0014-5793(71)80667-1. PMID: 11945635.
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On the specificity of neuraminidase The carboxymethyl alpha-ketoside of N-acetyl-D-neuraminic acid, a Vibrio cholerae neuraminidase substrate having two anionic sites.

FEBS letters

Holmquist L, Brossmer R.
PMID: 11946557
FEBS Lett. 1972 Apr 15;22(1):46-48. doi: 10.1016/0014-5793(72)80215-1.

No abstract available.

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Holmquist L, Brossmer R. On the specificity of neuraminidase The carboxymethyl alpha-ketoside of N-acetyl-D-neuraminic acid, a Vibrio cholerae neuraminidase substrate having two anionic sites. FEBS Lett. 1972;22(1):46-48doi: 10.1016/0014-5793(72)80215-1.
Holmquist, L., & Brossmer, R. (1972). On the specificity of neuraminidase The carboxymethyl alpha-ketoside of N-acetyl-D-neuraminic acid, a Vibrio cholerae neuraminidase substrate having two anionic sites. FEBS letters, 22(1), 46-48. https://doi.org/10.1016/0014-5793(72)80215-1
Holmquist, L, and Brossmer, R. "On the specificity of neuraminidase The carboxymethyl alpha-ketoside of N-acetyl-D-neuraminic acid, a Vibrio cholerae neuraminidase substrate having two anionic sites." FEBS letters vol. 22,1 (1972): 46-48. doi: https://doi.org/10.1016/0014-5793(72)80215-1
Holmquist L, Brossmer R. On the specificity of neuraminidase The carboxymethyl alpha-ketoside of N-acetyl-D-neuraminic acid, a Vibrio cholerae neuraminidase substrate having two anionic sites. FEBS Lett. 1972 Apr 15;22(1):46-48. doi: 10.1016/0014-5793(72)80215-1. PMID: 11946557.
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[No title available]

FEBS letters

Kleine R, Schubert J.
PMID: 11946635
FEBS Lett. 1972 May 15;22(3):352-355. doi: 10.1016/0014-5793(72)80268-0.

The high molecular weight arylamidase-alkaline phosphatase-complex from rat kidney microsomes [1] was carefully dissociated by means of treatment with several hydrolytic enzymes or by acidification. Trypsin, chymotrypsin and pronase cause a selective solubilization of the enzymes discernible at their...

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Kleine R, Schubert J. Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren. . FEBS Lett. 1972;22(3):352-355doi: 10.1016/0014-5793(72)80268-0.
Kleine, R., & Schubert, J. (1972). Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren. . FEBS letters, 22(3), 352-355. https://doi.org/10.1016/0014-5793(72)80268-0
Kleine, R, and Schubert, J. "Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren." . FEBS letters vol. 22,3 (1972): 352-355. doi: https://doi.org/10.1016/0014-5793(72)80268-0
Kleine R, Schubert J. Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren. . FEBS Lett. 1972 May 15;22(3):352-355. doi: 10.1016/0014-5793(72)80268-0. French. PMID: 11946635.
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