SECURITIES AND EXCHANGE COMMISSION

                             WASHINGTON, D.C. 20549

                                    FORM 8-K


                                 CURRENT REPORT

                     PURSUANT TO SECTION 13 OR 15(d) OF THE
                         SECURITIES EXCHANGE ACT OF 1934
                         Date of Report: August 17, 1999



                                 MEDIMMUNE, INC.
             (Exact name of registrant as specified in its charter)



                         Commission File Number: 0-19131




               Delaware                             52-1555759
       (State of Incorporation)        (I.R.S. Employer Identification No.)



                35 West Watkins Mill Road, Gaithersburg, MD 20878
                (Address of principal executive office (Zip Code)


Registrant's telephone number, including area code (301) 417-0770


No Exhibits are being filed with this report


CytoGam and RespiGam are  registered  trademarks of the Company and Synagis is a
trademark.


EDIMMUNE, INC.
MEDIMMUNE, INC.
Current Report on Form 8-K


ITEM 5.  OTHER EVENTS

MedImmune,  Inc.  reported  the  information  contained in the  following  press
release dated August 13, 1999:


FOR IMMEDIATE RELEASE
Contact:
William C. Roberts
Investor and Media Relations
MedImmune, Inc.
301-417-0770 x358

http://www.medimmune.com


<PAGE>

                 MEDIMMUNE ANNOUNCES NOVEL STRUCTURE OF URINARY
                         TRACT INFECTION VACCINE TARGET
           -X-ray Structure of FimC-FimH Complex Published in Science-

Gaithersburg,  MD,  August 13,  1999 --  MedImmune,  Inc.  (Nasdaq:  MEDI) today
announced that the x-ray structure of the FimC-FimH chaperone-adhesin complex of
uropathogenic  E.  coli has been  published  in the  August  13,  1999  issue of
Science.  The FimH adhesin,  the tip protein at the end of bacterial  pili which
facilitates  attachment and subsequent  colonization of E. coli to human bladder
tissue during  infection,  is required for colonization and antibody to FimH has
been shown to be protective  against E. coli  infection in a murine  model.  The
published  structural  data,  obtained  by Stefan D.  Knight,  Ph.D.,  associate
professor of molecular  biology,  and postdoctoral  fellow Devapriya  Choudhury,
Ph.D.,  both at  Uppsala  Biomedical  Center in  Sweden,  allows  scientists  to
correlate  structural  data with the Company's  ongoing  urinary tract infection
(UTI) vaccine work. MedImmune's research team, led by Solomon Langermann, Ph.D.,
is developing  its  candidate  vaccine for human use in  collaboration  with the
laboratories  of Scott  Hultgren,  Ph.D.,  at  Washington  University  School of
Medicine in St.  Louis and  Staffan  Normark,  M.D.,  Ph.D.,  at the  Karolinska
Institute in Stockholm, Sweden.

"This new structural data regarding the FimC-FimH chaperone-adhesin  interaction
will obviously provide valuable insight into the urinary tract infection vaccine
program,"   commented   Scott  J.  Hultgren,   Ph.D.,   professor  of  molecular
microbiology  at the  Washington  University  School of Medicine  in St.  Louis.
"Additionally, and perhaps most interestingly,  this data provides a new insight
into the paradigm of protein folding."

"These  data may  validate  MedImmune's  choice  of using the  entire  FimC-FimH
complex  as our E.  coli UTI  vaccine  candidate,  since  the FimC  molecule  is
required  to  direct  proper  folding  of  and to  stabilize  the  FimH  adhesin
structure,"  added Sol Langermann,  Ph.D.,  director of immunology and molecular
genetics at MedImmune.

The  article  in  Science  is  titled,   "X-ray   Structure  of  the   FimC-FimH
Chaperone-Adhesin  Complex from Uropathogenic E. coli." The FimH adhesin has two
major regions: One interacts with the FimC chaperone,  while the other interacts
with mannose,  a sugar attached to receptors in the lining of the bladder.  This
FimH-mannose   interaction  allows  the  bacterium  to  bind  and  colonize  the
urogenital tract.  Since this is the critical  interaction  during infection,  a
vaccine  targeting  this domain may mediate  protection  against  infection.  Of
particular  interest  in this study was the FimH  domain  which  allows  FimH to
interact  with  its  chaperone,   FimC.   This  domain  forms  a   barrel-shaped
immunoglobulin  fold, a structure  typically made up of seven strands.  However,
the FimH immunoglobulin  fold lacks one of the strands.  This forms a gap in the
FimH molecule,  which would render it unstable.  Scientists  discovered that the
FimC chaperone,  which also forms an immunoglobulin fold, temporarily shares its
seventh strand with the FimH subunit  without  actually  parting with the shared
strand in a process called "donor strand complementation".  This complementation
forms the FimC-FimH  complex which stabilizes and allows proper folding of FimH,
and explains the basis for  chaperone  function.  The  discovery of donor strand
complementation  provides a twist to the dogma of protein folding.  According to
the thermodynamic  hypothesis of 1972 Nobel-prize  winner Christian B. Anfinsen,
Ph.D.,  the three  dimensional  shapes of proteins are determined  solely by the
positions of the amino acid building blocks.  However,  this new data points out
that the structure of FimH is somewhat  determined by specific  interaction with
its chaperone.

UTIs are a  significant  medical  problem and one of the most  common  disorders
prompting  medical  attention in otherwise  healthy  women and  children.  It is
estimated  that by age 30  roughly  50  percent  of women  have had at least one
infection  and 2-10 percent are affected by  recurrent  infections.  Females are
generally  more prone to UTIs simply due to their  anatomy.  Recent studies have
shown that, on average,  women who are 18-40 years old get 1-2 infections over a
two-year period.  Older adults are also at risk with the incidence as high as 33
out of 100 people.  Most  infections  can be treated with  antibiotics,  however
recurrence  is common  and  emerging  antibiotic  resistant  bacteria  create an
additional threat.

MedImmune's  scientific  collaborators,  studying  the cause of UTI  infections,
found that bacteria establish infection in humans by using hair-like appendages,
called pili, to attach to bladder  cells.  The FimH adhesin,  the protein at the
tip  of  the  pili,  is  the  "anchor"  responsible  for  attachment.  MedImmune
scientists  have shown  that  vaccinating  mice with this  protein  can  produce
antibodies  that prevent  establishment  of a UTI in the animals when challenged
with disease-causing E. coli bacteria.  Furthermore,  the antibodies elicited by
the vaccine prevented the attachment to bladder cells of 94 percent of random E.
coli UTI isolates and 100 percent of isolates from women with  recurrent E. coli
infections tested in in vitro studies.

In  1998,  MedImmune  completed  a  vaccination  study  with  FimH in  non-human
primates. These studies demonstrated a dramatic decrease in bladder colonization
by E. coli in vaccinated animals.  The Company expects to complete  pre-clinical
development and file an investigational  new drug (IND) application with the FDA
to begin clinical trials with its FimC-FimH complex UTI vaccine candidate in the
fourth quarter of 1999.

MedImmune, located in Gaithersburg, Maryland, is a biotechnology company focused
on developing and marketing products that address medical needs in areas such as
infectious disease,  transplantation medicine,  autoimmune disorders and cancer.
MedImmune markets three products through its hospital-based  sales force and has
five new product candidates in clinical trials.

This announcement may contain,  in addition to historical  information,  certain
forward-looking statements that involve risks and uncertainties. Such statements
reflect management's current views and are based on certain assumptions.  Actual
results could differ materially from those currently  anticipated as a result of
a  number  of  factors,  including  risks  and  uncertainties  discussed  in the
Company's filings with the U.S. Securities and Exchange Commission.




                                 MEDIMMUNE, INC
                                  (REGISTRANT)



BY (SIGNATURE)                      /s/ David M. Mott
(NAME AND TITLE)                    David M. Mott, Vice Chairman and
                                    Chief Financial Officer
(DATE)                              August 17, 1999
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SECURITIES AND EXCHANGE COMMISSION

                             WASHINGTON, D.C. 20549

                                    FORM 8-K

                                 CURRENT REPORT

                     PURSUANT TO SECTION 13 OR 15(d) OF THE
                         SECURITIES EXCHANGE ACT OF 1934
                         Date of Report: August 17, 1999

                                 MEDIMMUNE, INC.
             (Exact name of registrant as specified in its charter)

                         Commission File Number: 0-19131

               Delaware                             52-1555759
       (State of Incorporation)        (I.R.S. Employer Identification No.)

                35 West Watkins Mill Road, Gaithersburg, MD 20878
                (Address of principal executive office (Zip Code)

Registrant's telephone number, including area code (301) 417-0770

No Exhibits are being filed with this report

CytoGam and RespiGam are  registered  trademarks of the Company and Synagis is a
trademark.

EDIMMUNE, INC.
MEDIMMUNE, INC.
Current Report on Form 8-K

ITEM 5.  OTHER EVENTS

MedImmune,  Inc.  reported  the  information  contained in the  following  press
release dated August 13, 1999:

FOR IMMEDIATE RELEASE
Contact:
William C. Roberts
Investor and Media Relations
MedImmune, Inc.
301-417-0770 x358

http://www.medimmune.com
MEDIMMUNE ANNOUNCES NOVEL STRUCTURE OF URINARY
                         TRACT INFECTION VACCINE TARGET
           -X-ray Structure of FimC-FimH Complex Published in Science-

Gaithersburg,  MD,  August 13,  1999 --  MedImmune,  Inc.  (Nasdaq:  MEDI) today
announced that the x-ray structure of the FimC-FimH chaperone-adhesin complex of
uropathogenic  E.  coli has been  published  in the  August  13,  1999  issue of
Science.  The FimH adhesin,  the tip protein at the end of bacterial  pili which
facilitates  attachment and subsequent  colonization of E. coli to human bladder
tissue during  infection,  is required for colonization and antibody to FimH has
been shown to be protective  against E. coli  infection in a murine  model.  The
published  structural  data,  obtained  by Stefan D.  Knight,  Ph.D.,  associate
professor of molecular  biology,  and postdoctoral  fellow Devapriya  Choudhury,
Ph.D.,  both at  Uppsala  Biomedical  Center in  Sweden,  allows  scientists  to
correlate  structural  data with the Company's  ongoing  urinary tract infection
(UTI) vaccine work. MedImmune's research team, led by Solomon Langermann, Ph.D.,
is developing  its  candidate  vaccine for human use in  collaboration  with the
laboratories  of Scott  Hultgren,  Ph.D.,  at  Washington  University  School of
Medicine in St.  Louis and  Staffan  Normark,  M.D.,  Ph.D.,  at the  Karolinska
Institute in Stockholm, Sweden.

"This new structural data regarding the FimC-FimH chaperone-adhesin  interaction
will obviously provide valuable insight into the urinary tract infection vaccine
program,"   commented   Scott  J.  Hultgren,   Ph.D.,   professor  of  molecular
microbiology  at the  Washington  University  School of Medicine  in St.  Louis.
"Additionally, and perhaps most interestingly,  this data provides a new insight
into the paradigm of protein folding."

"These  data may  validate  MedImmune's  choice  of using the  entire  FimC-FimH
complex  as our E.  coli UTI  vaccine  candidate,  since  the FimC  molecule  is
required  to  direct  proper  folding  of  and to  stabilize  the  FimH  adhesin
structure,"  added Sol Langermann,  Ph.D.,  director of immunology and molecular
genetics at MedImmune.

The  article  in  Science  is  titled,   "X-ray   Structure  of  the   FimC-FimH
Chaperone-Adhesin  Complex from Uropathogenic E. coli." The FimH adhesin has two
major regions: One interacts with the FimC chaperone,  while the other interacts
with mannose,  a sugar attached to receptors in the lining of the bladder.  This
FimH-mannose   interaction  allows  the  bacterium  to  bind  and  colonize  the
urogenital tract.  Since this is the critical  interaction  during infection,  a
vaccine  targeting  this domain may mediate  protection  against  infection.  Of
particular  interest  in this study was the FimH  domain  which  allows  FimH to
interact  with  its  chaperone,   FimC.   This  domain  forms  a   barrel-shaped
immunoglobulin  fold, a structure  typically made up of seven strands.  However,
the FimH immunoglobulin  fold lacks one of the strands.  This forms a gap in the
FimH molecule,  which would render it unstable.  Scientists  discovered that the
FimC chaperone,  which also forms an immunoglobulin fold, temporarily shares its
seventh strand with the FimH subunit  without  actually  parting with the shared
strand in a process called "donor strand complementation".  This complementation
forms the FimC-FimH  complex which stabilizes and allows proper folding of FimH,
and explains the basis for  chaperone  function.  The  discovery of donor strand
complementation  provides a twist to the dogma of protein folding.  According to
the thermodynamic  hypothesis of 1972 Nobel-prize  winner Christian B. Anfinsen,
Ph.D.,  the three  dimensional  shapes of proteins are determined  solely by the
positions of the amino acid building blocks.  However,  this new data points out
that the structure of FimH is somewhat  determined by specific  interaction with
its chaperone.

UTIs are a  significant  medical  problem and one of the most  common  disorders
prompting  medical  attention in otherwise  healthy  women and  children.  It is
estimated  that by age 30  roughly  50  percent  of women  have had at least one
infection  and 2-10 percent are affected by  recurrent  infections.  Females are
generally  more prone to UTIs simply due to their  anatomy.  Recent studies have
shown that, on average,  women who are 18-40 years old get 1-2 infections over a
two-year period.  Older adults are also at risk with the incidence as high as 33
out of 100 people.  Most  infections  can be treated with  antibiotics,  however
recurrence  is common  and  emerging  antibiotic  resistant  bacteria  create an
additional threat.

MedImmune's  scientific  collaborators,  studying  the cause of UTI  infections,
found that bacteria establish infection in humans by using hair-like appendages,
called pili, to attach to bladder  cells.  The FimH adhesin,  the protein at the
tip  of  the  pili,  is  the  "anchor"  responsible  for  attachment.  MedImmune
scientists  have shown  that  vaccinating  mice with this  protein  can  produce
antibodies  that prevent  establishment  of a UTI in the animals when challenged
with disease-causing E. coli bacteria.  Furthermore,  the antibodies elicited by
the vaccine prevented the attachment to bladder cells of 94 percent of random E.
coli UTI isolates and 100 percent of isolates from women with  recurrent E. coli
infections tested in in vitro studies.

In  1998,  MedImmune  completed  a  vaccination  study  with  FimH in  non-human
primates. These studies demonstrated a dramatic decrease in bladder colonization
by E. coli in vaccinated animals.  The Company expects to complete  pre-clinical
development and file an investigational  new drug (IND) application with the FDA
to begin clinical trials with its FimC-FimH complex UTI vaccine candidate in the
fourth quarter of 1999.

MedImmune, located in Gaithersburg, Maryland, is a biotechnology company focused
on developing and marketing products that address medical needs in areas such as
infectious disease,  transplantation medicine,  autoimmune disorders and cancer.
MedImmune markets three products through its hospital-based  sales force and has
five new product candidates in clinical trials.

This announcement may contain,  in addition to historical  information,  certain
forward-looking statements that involve risks and uncertainties. Such statements
reflect management's current views and are based on certain assumptions.  Actual
results could differ materially from those currently  anticipated as a result of
a  number  of  factors,  including  risks  and  uncertainties  discussed  in the
Company's filings with the U.S. Securities and Exchange Commission.

                                 MEDIMMUNE, INC
                                  (REGISTRANT)

BY (SIGNATURE)                      /s/ David M. Mott
(NAME AND TITLE)                    David M. Mott, Vice Chairman and
                                    Chief Financial Officer
(DATE)                              August 17, 1999