NEWS RELEASE 30-APR-2020

Cracking the Lyme disease code

WASHINGTON STATE UNIVERSITY

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IMAGE: THIS IS ABDUL LONE. view more

CREDIT: WSU

The next time a tick feeds on you, Washington State University
researchers hope to make sure persistent arthritis caused by Lyme
disease doesn’t linger for a lifetime.

Troy Bankhead, associate professor in WSU’s Veterinary Microbiology
and Pathology department, and his team have spent more than a decade
analyzing an immune evasive protein of Borrelia burgdorferi, the
bacterium that causes tick-borne Lyme disease.

With the lab’s latest finding, that work is beginning to pay off.

According to research recently published in Cell Reports, Bankhead and
assistant research professor Abdul Lone discovered that a surface
protein known as VlsE acts as a shield to prevent the immune system
from effectively fighting the disease. In particular, the study
examined how VlsE protects one of the main proteins responsible for
Lyme disease’s persistent arthritis.

“This really has a significant impact in the development of vaccines,”
Bankhead said. “If we can determine which proteins are shielded as
opposed to which ones are not, then of course those that are not
protected are going to be better candidates for a vaccine.”

The Centers for Disease Control and Prevention estimates some 300,000
people may get Lyme disease each year in the United States alone. It
is most prevalent in the northeast.

If not treated early with antibiotics, Lyme disease can cause lifelong
arthritis, and in more severe cases, bladder infections, heart
inflammation, and neurologic and cognitive issues like loss of memory
and balance.

“We chose the arthritis-related protein because arthritis is the most
common symptom you see in North America,” Lone said.

By engineering a strain of Borrelia burgdorferi in the lab without the
surface lipoprotein VlsE, they were able to confirm it was protecting
the arthritis-related protein from an antibody response.

Bankhead and Lone tested the new Borrelia strain in mice and found the
animals were more easily able to clear the infection.

Then, Bankhead and Lone confirmed that the new Borrelia strain was
susceptible to antibodies under the microscope.

By using fluorescence microscopy, a process that uses energy from
electrons to emit light under a microscope, Bankhead and Lone watched
as antibodies were unable to bind to the protein responsible for
Lyme’s persistent arthritis when the VlsE protein was present.

When the VlsE protein was removed, antibodies were able to recognize
and bind to the arthritis-related protein. “When you don’t have VlsE
those bacteria light up and that is because those antibodies are able
to bind and recognize that arthritis-related protein in the absence of
that VlsE shield,” Bankhead said. “That’s exactly what we were
seeing.”

Understanding the VlsE protein is acting as a shield for the
bacterium’s arthritic-causing protein is significant for vaccine
development and future research. While it is unknown if other surface
proteins are protected, Bankhead said it is likely. He noted the
scientific community is gaining ground on understanding these proteins
but producing any vaccine is well into the future.

Still, the finding creates two avenues for researchers to eliminate
Lyme disease: take down the VlsE shield, or, find a way for the
antibody response to get in front of the ever-adapting bacterium and
eliminate it.

“HIV/AIDS persists for years in human beings. The same thing happens
with Borrelia, it persists,” Lone said. “While this finding tells us a
lot about Borrelia. Our next step is to understand how it persists.
Once we understand the mechanism of persistence, we can eliminate the
disease.”