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HEALTH CARE NEWS

US Congress extends CHIP, funds opioid crisis response following temporary shutdown

Publish date: February 9, 2018

By 

Gregory Twachtman 

Oncology Practice

 

 

 

 

 

 

 

 

 

Congress, despite a second shutdown in less than a month, was able to pass a number of financial extenders to fund key health care programs.

The bipartisan spending bill (H.R. 1892), passed in the early morning hours on Feb. 9 by a 71-28 vote in the Senate (16 Republicans and 12 Democrats voted against it, and Sen. John McCain [R-Ariz.] was not present) and a 240-186 vote in the House (67 Republicans and 119 Democrats voted against and 5 representatives did not vote). President Trump signed the bill later that morning.

 

The spending bill and continuing resolution to fund the government through March 23 includes $6 billion to fund treatment for opioid addiction and other mental health issues, $2 billion in additional funding for the National Institutes of Health, and 4 additional years of funding for the Children’s Health Insurance Program. The additional CHIP funding extends the program for a total of 10 years.

The funding bill also made a technical correction to the Merit-based Incentive Payment System (MIPS) track of the Medicare Quality Payment Program. It removes Part B drug reimbursement from the MIPS payment adjustment, so any positive or negative change to physician payments based on the MIPS score will only be applied to physician fee schedule payments.

The bill also repeals the Independent Payment Advisory Board, a panel created by the Affordable Care Act that would have the power to slash Medicare spending under certain budget circumstances. That board was never convened.

The funding legislation also accelerates closure of the Medicare Part D “donut hole,” the coverage gap in which beneficiaries must pay 100% of medication costs prior to entering catastrophic coverage.

Just over $7 billion was provided for community health centers and Medicare’s therapy caps were repealed.

While the funding bill was written in the Senate with bipartisan input and received bipartisan support, Sen. Rand Paul (R-Ky.) held up votes over objections to the more than $1 trillion it will add to the nation’s debt, as well as for the fact that there was no opportunity to introduce and vote on amendments, leading to an hours-long government shutdown.

There also were concerns about two issues that could have derailed the vote in the House. Democrats wanted to add language to address immigrants brought to this nation illegally as children, while some Republicans did not want to increase the federal debt. However, there were enough votes to pass the funding legislation.

gtwachtman@frontlinemedcom.com

For a Better Influenza Vaccine, Focus on the Neglected “N”

Drotumdi O

 For a Better Influenza Vaccine, Focus on the Neglected “N”  Targeting neuraminidase—the “N” in H1N1—could help prevent the flu and limit severity     Article ID: 691995  Released: 30-Mar-2018 11:05 AM EDT  Source Newsroom:  University of Chicago Medical Center    Add to Favorites         more news from this source    contact patient services             Share                  Credit: The University of Chicago Medicine  Patrick Wilson, who led the UChicago Medicine team, and study co-author Nai-Ying Zheng in a laboratory in the Knapp Center for Lupus and Immunology Research at the University of Chicago           Credit: The Wilson laboratory  A schematic of the influenza virus surface where the blue tetramers are the neuraminidase glycoprotein and the brown trimers are the hemagglutinin glycoprotein.           Credit: Wikimedia Commons:  A ribbon model of the structure of influenza neuraminidase glycoprotein. The Wilson and Krammer laboratories found that maintaining the structure of neuraminidase during the production of future influenza vaccines could substantially improve protection from influenza infection.           Credit: The University of Chicago Medicine  Patrick Wilson, who led the UChicago Medicine team, and study co-author Nai-Ying Zheng in a laboratory in the Knapp Center for Lupus and Immunology Research at the University of Chicago           Credit: The Wilson laboratory  A schematic of the influenza virus surface where the blue tetramers are the neuraminidase glycoprotein and the brown trimers are the hemagglutinin glycoprotein.   Prev  Next      MEDIA CONTACT   Available for logged-in reporters only   CITATIONS   Cell, April 5, 2018   CHANNELS   All Journal News ,  Cell Biology ,  Infectious Diseases ,  Vaccines ,  Influenza ,  Cell (journal) ,  Local - Illinois   KEYWORDS   Influenza ,  Influenca vaccine ,  Neuraminidase ,  Hemagglutinin ,  Viral-surface glycoproteins  ,   Viral cellular egress ,  Shifting focus to neuraminidase ,  Vaccine effectiveness ,  Neutralize neuraminidase ,  Antibodies   + Show More        Newswise — Vaccines designed to protect people from the influenza virus tend to concentrate on hemagglutinin, one of the two prominently displayed proteins on the surface of the virus and the primary target for influenza prevention.  In the April 5, 2018, issue of the journal  Cell , however, teams led by Patrick Wilson at the University of Chicago Medicine and Florian Krammer at the Icahn School of Medicine at Mt. Sinai Hospital in New York City argue that placing greater emphasis on the comparatively neglected protein, neuraminidase, could substantially decrease infection rates and reduce disease severity for those infected with the virus.  These two viral-surface glycoproteins have distinct roles. Hemagglutinin enables the virus to attach to a host’s cell membranes and enter that person’s cells. Once inside the cell, the virus makes multiple copies of itself. These copies then prepare to burst out of their hijacked cell and infect more cells.  The virus cannot get out of the cell, however, without help from the other protein. Neuraminidase facilitates egress. It enables newly formed viral particles to escape the original cell and infect nearby cells, where they multiply again, repeating the process and allowing the infection to spread rapidly throughout the body.  “Hemagglutinin activity has been the primary measure of influenza-vaccine efficacy for decades,” said Wilson, the study’s senior author and a professor of medicine at the University of Chicago. The current anti-flu vaccines concentrate on hemagglutinin. “But they do a poor job of stimulating the immune system to neutralize neuraminidase,” Wilson said. “Neuraminidase, one of two prime targets, has been profoundly neglected. This leaves a big hole in immunity.”  Interim estimates from the Centers for Disease Control and Prevention confirm the need for a more trustworthy vaccine. The U.S. Influenza Vaccine Effectiveness survey found that the vaccine’s ability to protect people from influenza A or B during the period from November 2, 2017, to February 3, 2018, was a dismal 36 percent. That fell to 25 percent for the influenza A (H3N2) virus. In the previous three influenza seasons, effectiveness ranged from a low of 19 percent to a high of 48 percent.  So Wilson and colleagues focused instead on the neglected link. Neuraminidase is “highly immunogenic,” he said. Infection induces nearly equal numbers of neuraminidase and hemagglutinin-reactive B cells. These cells produce the crucial antibodies that block activity of flu-related viral proteins.  But the current vaccines rarely trigger an effective response from neuraminidase-reactive B cells. “The hemagglutinin tends to maintain its structure,” Wilson said, “but the neuraminidase, a more complicated, delicate four-part structure, breaks down. It sort of falls apart.”  As a result, the antibodies that should neutralize neuraminidase, locking potentially virulent viral particles inside infected cells, are much less effective. In many cases, the neuraminidase component of the vaccines triggers antibody production at levels “nearly 90-fold lower,” the authors note, than antibodies aimed at hemagglutinin.  “The current vaccines rely on sub-units, small pieces of the neuraminidase protein, rather than the full target,” Wilson said. “The current process of inactivating the vaccine seems to destroy the neuraminidase protein.”  When the researchers tested monoclonal antibodies collected from unvaccinated mice that were infected with influenza, they found that those antibodies could provide robust protection. Even when given to mice 48 hours after infection with the virus, the neuraminidase-reactive antibodies were effective at levels comparable to the hemagglutinin-reactive antibodies, protecting the mice from a lethal influenza challenge.  “Our results demonstrate that hemagglutinin should no longer be the de-facto target in influenza vaccine development efforts,” Wilson said. “We think including an improved neuraminidase component to future influenza vaccine compositions can reduce the severity of illness and decrease the frequency of community-acquired influenza infections.”   “With a robust response to neuraminidase,” the authors conclude, “the degree of protection conferred might protect from any influenza infection.” It could even provide “broad-ranging protection,” they suggest, “against potential pandemic strains that express N1 or N2 neuraminidases.”  ###  The study, “Influenza infection in humans induces broadly cross-reactive and protective neuraminidase-reactive antibodies,” was supported by the National Institute of Allergy and Infectious Diseases and the Food and Drug Administration.  Additional authors were first author Yaoqing Chen, Nai-Ying Zheng, Min Huang, Yunpint Huang, Karla Rojas, Carole Henry, Anna-Karin Palm, Karlynn Neu, Christopher Stamper and Linda Lan from the University of Chicago; Florian Krammer, John Wohlbold and Erika Kirkpatrick from the Icahn Scool of Medicine at Mt. Sinai; Jiwon Lee and George Georgiou from the University of Texas at Austin; Hongquan Wan and Maryna Eichelberger from the Food and Drug Administration; David Topham and John Treanor from the University of Rochester; and Jens Wrammert and Rafi Ahmen from Emory University. DOI: 10.1016/j.cell.2018.03.030        Permalink to this article               COMMENTS  |  COMMENTING POLICY   We recommend   Antibodies Triggered by Avian Influenza Virus Vaccine Illuminate a New Path Toward a Universal Flu Vaccine   Newswise   Seasonal Flu Vaccine Induces Antibodies That Protect Against H7N9 Avian Flu   Newswise   Vaccines Fail to Protect Obese Mice From Severe Influenza Infections   Newswise   The Flu Gets Cold   Newswise   Pre-Existing Immunity to Dengue and West Nile Viruses May Cause Increased Risk in Zika-Infected   Newswise      Share your Insights and Learn How Readers Discover Content   TrendMD, Renew Publishing Consultants   Yale Researchers Find Host mRNA, Protein Biomarkers Predictive of Viral Infections   360Dx   Hepatitis C Remission   Healthline   A humble chicken virus that changed biology and medicine   Peter K Vogt, The Lancet Oncology   FDA Reclassification of Rapid Flu Tests Forces Changes in Technology   360Dx   Powered by TrendMD        View All Latest News

For a Better Influenza Vaccine, Focus on the Neglected “N”

Targeting neuraminidase—the “N” in H1N1—could help prevent the flu and limit severity

Article ID: 691995

Released: 30-Mar-2018 11:05 AM EDT

Source Newsroom: University of Chicago Medical Center

Add to Favorites

more news from this source

contact patient services

 

Share

 

Credit: The University of Chicago Medicine

Patrick Wilson, who led the UChicago Medicine team, and study co-author Nai-Ying Zheng in a laboratory in the Knapp Center for Lupus and Immunology Research at the University of Chicago

 

Credit: The Wilson laboratory

A schematic of the influenza virus surface where the blue tetramers are the neuraminidase glycoprotein and the brown trimers are the hemagglutinin glycoprotein.

 

Credit: Wikimedia Commons:

A ribbon model of the structure of influenza neuraminidase glycoprotein. The Wilson and Krammer laboratories found that maintaining the structure of neuraminidase during the production of future influenza vaccines could substantially improve protection from influenza infection.

 

Credit: The University of Chicago Medicine

Patrick Wilson, who led the UChicago Medicine team, and study co-author Nai-Ying Zheng in a laboratory in the Knapp Center for Lupus and Immunology Research at the University of Chicago

 

Credit: The Wilson laboratory

A schematic of the influenza virus surface where the blue tetramers are the neuraminidase glycoprotein and the brown trimers are the hemagglutinin glycoprotein.

PrevNext

MEDIA CONTACT

Available for logged-in reporters only

CITATIONS

Cell, April 5, 2018

CHANNELS

All Journal News, Cell Biology, Infectious Diseases, Vaccines, Influenza, Cell (journal), Local - Illinois

KEYWORDS

Influenza, Influenca vaccine, Neuraminidase, Hemagglutinin, Viral-surface glycoproteins ,

Viral cellular egress, Shifting focus to neuraminidase, Vaccine effectiveness, Neutralize neuraminidase, Antibodies

+ Show More

 

Newswise — Vaccines designed to protect people from the influenza virus tend to concentrate on hemagglutinin, one of the two prominently displayed proteins on the surface of the virus and the primary target for influenza prevention.

In the April 5, 2018, issue of the journal Cell, however, teams led by Patrick Wilson at the University of Chicago Medicine and Florian Krammer at the Icahn School of Medicine at Mt. Sinai Hospital in New York City argue that placing greater emphasis on the comparatively neglected protein, neuraminidase, could substantially decrease infection rates and reduce disease severity for those infected with the virus.

These two viral-surface glycoproteins have distinct roles. Hemagglutinin enables the virus to attach to a host’s cell membranes and enter that person’s cells. Once inside the cell, the virus makes multiple copies of itself. These copies then prepare to burst out of their hijacked cell and infect more cells.

The virus cannot get out of the cell, however, without help from the other protein. Neuraminidase facilitates egress. It enables newly formed viral particles to escape the original cell and infect nearby cells, where they multiply again, repeating the process and allowing the infection to spread rapidly throughout the body.

“Hemagglutinin activity has been the primary measure of influenza-vaccine efficacy for decades,” said Wilson, the study’s senior author and a professor of medicine at the University of Chicago. The current anti-flu vaccines concentrate on hemagglutinin. “But they do a poor job of stimulating the immune system to neutralize neuraminidase,” Wilson said. “Neuraminidase, one of two prime targets, has been profoundly neglected. This leaves a big hole in immunity.”

Interim estimates from the Centers for Disease Control and Prevention confirm the need for a more trustworthy vaccine. The U.S. Influenza Vaccine Effectiveness survey found that the vaccine’s ability to protect people from influenza A or B during the period from November 2, 2017, to February 3, 2018, was a dismal 36 percent. That fell to 25 percent for the influenza A (H3N2) virus. In the previous three influenza seasons, effectiveness ranged from a low of 19 percent to a high of 48 percent.

So Wilson and colleagues focused instead on the neglected link. Neuraminidase is “highly immunogenic,” he said. Infection induces nearly equal numbers of neuraminidase and hemagglutinin-reactive B cells. These cells produce the crucial antibodies that block activity of flu-related viral proteins.

But the current vaccines rarely trigger an effective response from neuraminidase-reactive B cells. “The hemagglutinin tends to maintain its structure,” Wilson said, “but the neuraminidase, a more complicated, delicate four-part structure, breaks down. It sort of falls apart.”

As a result, the antibodies that should neutralize neuraminidase, locking potentially virulent viral particles inside infected cells, are much less effective. In many cases, the neuraminidase component of the vaccines triggers antibody production at levels “nearly 90-fold lower,” the authors note, than antibodies aimed at hemagglutinin.

“The current vaccines rely on sub-units, small pieces of the neuraminidase protein, rather than the full target,” Wilson said. “The current process of inactivating the vaccine seems to destroy the neuraminidase protein.”

When the researchers tested monoclonal antibodies collected from unvaccinated mice that were infected with influenza, they found that those antibodies could provide robust protection. Even when given to mice 48 hours after infection with the virus, the neuraminidase-reactive antibodies were effective at levels comparable to the hemagglutinin-reactive antibodies, protecting the mice from a lethal influenza challenge.

“Our results demonstrate that hemagglutinin should no longer be the de-facto target in influenza vaccine development efforts,” Wilson said. “We think including an improved neuraminidase component to future influenza vaccine compositions can reduce the severity of illness and decrease the frequency of community-acquired influenza infections.” 

“With a robust response to neuraminidase,” the authors conclude, “the degree of protection conferred might protect from any influenza infection.” It could even provide “broad-ranging protection,” they suggest, “against potential pandemic strains that express N1 or N2 neuraminidases.”

###

The study, “Influenza infection in humans induces broadly cross-reactive and protective neuraminidase-reactive antibodies,” was supported by the National Institute of Allergy and Infectious Diseases and the Food and Drug Administration.

Additional authors were first author Yaoqing Chen, Nai-Ying Zheng, Min Huang, Yunpint Huang, Karla Rojas, Carole Henry, Anna-Karin Palm, Karlynn Neu, Christopher Stamper and Linda Lan from the University of Chicago; Florian Krammer, John Wohlbold and Erika Kirkpatrick from the Icahn Scool of Medicine at Mt. Sinai; Jiwon Lee and George Georgiou from the University of Texas at Austin; Hongquan Wan and Maryna Eichelberger from the Food and Drug Administration; David Topham and John Treanor from the University of Rochester; and Jens Wrammert and Rafi Ahmen from Emory University. DOI: 10.1016/j.cell.2018.03.030

 

Permalink to this article

 

 

COMMENTS | COMMENTING POLICY

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